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Conserved domains on  [gi|237681200|ref|NP_001153737|]
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cytochrome P450 2W1 precursor [Mus musculus]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

cytochrome P450 family protein may catalyze the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
66-487 0e+00

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


The actual alignment was detected with superfamily member cd20671:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 422  Bit Score: 794.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPR 225
Cdd:cd20671   81 IEDKILEELQFLNGQIDSFNGKPFPLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 226 LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPtGGPAQSYVEALLQQGQEDDP-EDMFGEANVLACTLDMVMAGTETT 304
Cdd:cd20671  161 LGAFLKLHKPILDKVEEVCMILRTLIEARRPTID-GNPLHSYIEALIQKQEEDDPkETLFHDANVLACTLDLVMAGTETT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 305 AATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPK 384
Cdd:cd20671  240 STTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 385 GTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPG 464
Cdd:cd20671  320 GTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPG 399
                        410       420
                 ....*....|....*....|...
gi 237681200 465 LSPADLDLRPAPAFTMRPPAQTL 487
Cdd:cd20671  400 VSPADLDATPAAAFTMRPQPQLL 422
 
Name Accession Description Interval E-value
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
66-487 0e+00

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 794.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPR 225
Cdd:cd20671   81 IEDKILEELQFLNGQIDSFNGKPFPLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 226 LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPtGGPAQSYVEALLQQGQEDDP-EDMFGEANVLACTLDMVMAGTETT 304
Cdd:cd20671  161 LGAFLKLHKPILDKVEEVCMILRTLIEARRPTID-GNPLHSYIEALIQKQEEDDPkETLFHDANVLACTLDLVMAGTETT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 305 AATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPK 384
Cdd:cd20671  240 STTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 385 GTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPG 464
Cdd:cd20671  320 GTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPG 399
                        410       420
                 ....*....|....*....|...
gi 237681200 465 LSPADLDLRPAPAFTMRPPAQTL 487
Cdd:cd20671  400 VSPADLDATPAAAFTMRPQPQLL 422
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-489 5.71e-124

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 369.69  E-value: 5.71e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200   35 PPGPRPLPFLGNLHLLGVTQQ-DRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQ- 112
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNlHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  113 --RGGGIFFSSGARWRAGRQFTVRTLQSLGVQqpSMVGKVLQELACLKGQLDSYGGQPL---PLALLGWAPCNITFTLLF 187
Cdd:pfam00067  81 pfLGKGIVFANGPRWRQLRRFLTPTFTSFGKL--SFEPRVEEEARDLVEKLRKTAGEPGvidITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  188 GQRFD-YQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVR--TILRTLLETRRPPLPTGGPA 264
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIkdLLDKLIEERRETLDSAKKSP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  265 QSYVEALLQqGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQ 344
Cdd:pfam00067 239 RDFLDALLL-AKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  345 RALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKR 423
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKS 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237681200  424 GAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRpaPAFTMRPPAQTLCV 489
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET--PGLLLPPKPYKLKF 461
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
35-470 5.55e-49

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 175.69  E-value: 5.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  35 PPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQhIQRG 114
Cdd:PLN02394  32 PPGPAAVPIFGNWLQVGDDLNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD-IFTG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 115 GG---IFFSSGARWRAGRQ------FTVRTLQSLGVQQPSMVGKVLQELaclKGQLDSYGG-----QPLPLALLgwapcN 180
Cdd:PLN02394 111 KGqdmVFTVYGDHWRKMRRimtvpfFTNKVVQQYRYGWEEEADLVVEDV---RANPEAATEgvvirRRLQLMMY-----N 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 181 ITFTLLFGQRFDYQ-DPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHrpvLSKIEEVRTILRTL-----LETR 254
Cdd:PLN02394 183 IMYRMMFDRRFESEdDPLFLKLKALNGERSRLAQSFEYNYGDFIPILRPFLRGY---LKICQDVKERRLALfkdyfVDER 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 255 RPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLG 334
Cdd:PLN02394 260 KKLMSAKGMDKEGLKCAIDHILEAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLG 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 335 PG-QLPQPEHQRaLPYTSAVLHEVQRY---ITLLphVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNP 410
Cdd:PLN02394 340 PGnQVTEPDTHK-LPYLQAVVKETLRLhmaIPLL--VPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRP 416
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237681200 411 NHFLDAKGRFMKRGA---FLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADL 470
Cdd:PLN02394 417 ERFLEEEAKVEANGNdfrFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQSKIDV 479
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
25-484 3.71e-42

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 154.67  E-value: 3.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  25 TRSPSLAPRWPPGPR----PLPFLGNLHllgvtqqdralmelseRYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELA 100
Cdd:COG2124    2 TATATPAADLPLDPAflrdPYPFYARLR----------------EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 101 DRPPIPIFQHIQR-GGGIFFSSGARWRAGRQ-----FTVRTLQSLGvqqPSMVGKVLQELACL--KGQLDSYG--GQPLP 170
Cdd:COG2124   66 DGGLPEVLRPLPLlGDSLLTLDGPEHTRLRRlvqpaFTPRRVAALR---PRIREIADELLDRLaaRGPVDLVEefARPLP 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 171 LallgwapcnITFTLLFGQRFDYQDPvfvsLLSLIDQVMVLLGSPgiqlfnTFPRLGAFLRLHRpvlskieEVRTILRTL 250
Cdd:COG2124  143 V---------IVICELLGVPEEDRDR----LRRWSDALLDALGPL------PPERRRRARRARA-------ELDAYLREL 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 251 LETRRpplptGGPAQSYVEALLQqgQEDDPEDMfGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEld 330
Cdd:COG2124  197 IAERR-----AEPGDDLLSALLA--ARDDGERL-SDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-- 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 331 rvlgpgqlpqpehqraLPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNP 410
Cdd:COG2124  267 ----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDP 330
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237681200 411 nhfldakGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYrllppPGLSPA-DLDLRPAPAFTMRPPA 484
Cdd:COG2124  331 -------DR--PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRF-----PDLRLApPEELRWRPSLTLRGPK 391
 
Name Accession Description Interval E-value
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
66-487 0e+00

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 794.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPR 225
Cdd:cd20671   81 IEDKILEELQFLNGQIDSFNGKPFPLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 226 LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPtGGPAQSYVEALLQQGQEDDP-EDMFGEANVLACTLDMVMAGTETT 304
Cdd:cd20671  161 LGAFLKLHKPILDKVEEVCMILRTLIEARRPTID-GNPLHSYIEALIQKQEEDDPkETLFHDANVLACTLDLVMAGTETT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 305 AATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPK 384
Cdd:cd20671  240 STTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPK 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 385 GTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPG 464
Cdd:cd20671  320 GTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPG 399
                        410       420
                 ....*....|....*....|...
gi 237681200 465 LSPADLDLRPAPAFTMRPPAQTL 487
Cdd:cd20671  400 VSPADLDATPAAAFTMRPQPQLL 422
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
66-487 0e+00

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 548.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd11026   81 IEERIQEEAKFLVEAFRKTKGKPFdPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 R-LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLpTGGPAQSYVEALLQQGQE--DDPEDMFGEANVLACTLDMVMAGT 301
Cdd:cd11026  161 PlLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETL-DPSSPRDFIDCFLLKMEKekDNPNSEFHEENLVMTVLDLFFAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 302 ETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGY 380
Cdd:cd11026  240 ETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPlGVPHAVTRDTKFRGY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLL 460
Cdd:cd11026  320 TIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLS 399
                        410       420
                 ....*....|....*....|....*...
gi 237681200 461 PPPGlsPADLDLRPA-PAFTMRPPAQTL 487
Cdd:cd11026  400 SPVG--PKDPDLTPRfSGFTNSPRPYQL 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
66-487 4.65e-158

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 455.42  E-value: 4.65e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPLPLAL-LGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20664   81 SEDKILEEIPYLIEVFEKHKGKPFETTLsMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPaQSYVEA-LLQQGQEDDPEDMFGEANVLACTL-DMVMAGTE 302
Cdd:cd20664  161 WLGPFPGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQ-RGFIDAfLVKQQEEEESSDSFFHDDNLTCSVgNLFGAGTD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 303 TTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQlPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYL 381
Cdd:cd20664  240 TTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQ-PQVEHRKNMPYTDAVIHEIQRFANIVPmNLPHATTRDVTFRGYF 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 382 LPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP 461
Cdd:cd20664  319 IPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP 398
                        410       420
                 ....*....|....*....|....*.
gi 237681200 462 PPGLSPADLDLRPAPAFTMRPPAQTL 487
Cdd:cd20664  399 PPGVSEDDLDLTPGLGFTLNPLPHQL 424
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
66-483 9.39e-136

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 398.56  E-value: 9.39e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20665    1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20665   81 IEDRVQEEARCLVEELRKTNGSPCdPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLR-LHRPVLSKIEEVRTILRTLLETRRPPLPTGGPaQSYVEALL-QQGQEDDPEDM-FGEANVLACTLDMVMAGT 301
Cdd:cd20665  161 ALLDYLPgSHNKLLKNVAYIKSYILEKVKEHQESLDVNNP-RDFIDCFLiKMEQEKHNQQSeFTLENLAVTVTDLFGAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 302 ETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGY 380
Cdd:cd20665  240 ETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPnNLPHAVTCDTKFRNY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLl 460
Cdd:cd20665  320 LIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNL- 398
                        410       420
                 ....*....|....*....|....
gi 237681200 461 pPPGLSPADLDLRPAP-AFTMRPP 483
Cdd:cd20665  399 -KSLVDPKDIDTTPVVnGFASVPP 421
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-489 5.71e-124

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 369.69  E-value: 5.71e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200   35 PPGPRPLPFLGNLHLLGVTQQ-DRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQ- 112
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNlHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  113 --RGGGIFFSSGARWRAGRQFTVRTLQSLGVQqpSMVGKVLQELACLKGQLDSYGGQPL---PLALLGWAPCNITFTLLF 187
Cdd:pfam00067  81 pfLGKGIVFANGPRWRQLRRFLTPTFTSFGKL--SFEPRVEEEARDLVEKLRKTAGEPGvidITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  188 GQRFD-YQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVR--TILRTLLETRRPPLPTGGPA 264
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIkdLLDKLIEERRETLDSAKKSP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  265 QSYVEALLQqGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQ 344
Cdd:pfam00067 239 RDFLDALLL-AKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  345 RALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKR 423
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKS 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237681200  424 GAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRpaPAFTMRPPAQTLCV 489
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET--PGLLLPPKPYKLKF 461
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
66-482 7.50e-123

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 365.66  E-value: 7.50e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20662   81 LEERIQEECRHLVEAIREEKGNPFnPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLR-LHRPVLSKIEEVRTILRTLLETRRPPLPTGGPaQSYVEALLQQGQED-DPEDMFGEANVLACTLDMVMAGTE 302
Cdd:cd20662  161 WIMKYLPgSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEP-RDFIDAYLKEMAKYpDPTTSFNEENLICSTLDLFFAGTE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 303 TTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYL 381
Cdd:cd20662  240 TTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPlNVPREVAVDTKLAGFH 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 382 LPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDaKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP 461
Cdd:cd20662  320 LPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE-NGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKP 398
                        410       420
                 ....*....|....*....|.
gi 237681200 462 PPGlspADLDLRPAPAFTMRP 482
Cdd:cd20662  399 PPN---EKLSLKFRMGITLSP 416
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
66-474 1.03e-117

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 352.53  E-value: 1.03e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFdPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLR-LHRPVLSKIEEVRTILRTLLETRRPPLPTGGPaQSYVEALLQQGQED--DPEDMFGEANVLACTLDMVMAGT 301
Cdd:cd20669  161 SVMDWLPgPHQRIFQNFEKLRDFIAESVREHQESLDPNSP-RDFIDCFLTKMAEEkqDPLSHFNMETLVMTTHNLLFGGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 302 ETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGY 380
Cdd:cd20669  240 ETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNFRGF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLL 460
Cdd:cd20669  320 LIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
                        410
                 ....*....|....
gi 237681200 461 PPpgLSPADLDLRP 474
Cdd:cd20669  400 PL--GAPEDIDLTP 411
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
66-482 6.99e-116

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 347.84  E-value: 6.99e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGG---GIFFSS-GARWRAGRQFTVRTLQSLGV 141
Cdd:cd20663    1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPksqGVVLARyGPAWREQRRFSVSTLRNFGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 142 QQPSMVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLF 220
Cdd:cd20663   81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFnPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 221 NTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQE--DDPEDMFGEANVLACTLDMVM 298
Cdd:cd20663  161 NAFPVLLRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLTDAFLAEMEKakGNPESSFNDENLRLVVADLFS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 299 AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQL 377
Cdd:cd20663  241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPlGVPHMTSRDIEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 378 GGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRY 457
Cdd:cd20663  321 QGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
                        410       420
                 ....*....|....*....|....*.
gi 237681200 458 RLLPPPGL-SPADldlRPAPAFTMRP 482
Cdd:cd20663  401 SFSVPAGQpRPSD---HGVFAFLVSP 423
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
66-470 9.97e-109

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 329.56  E-value: 9.97e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGG-GIFFSS-GARWRAGRQFTVRTLQSLGVQQ 143
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGkDIAFGDySPTWKLHRKLAHSALRLYASGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 144 PSMVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSlIDQVMVLLGSPGIQLfNT 222
Cdd:cd11027   81 PRLEEKIAEEAEKLLKRLASQEGQPFdPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLD-LNDKFFELLGAGSLL-DI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPRLGAF-LRLHRPVLSKIEEVRTILRTLLETRRPPLpTGGPAQSYVEALLQQGQE-----DDPEDMFGEANVLACTLDM 296
Cdd:cd11027  159 FPFLKYFpNKALRELKELMKERDEILRKKLEEHKETF-DPGNIRDLTDALIKAKKEaedegDEDSGLLTDDHLVMTISDI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 297 VMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADI 375
Cdd:cd11027  238 FGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPlALPHKTTCDT 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFM-KRGAFLPFSAGRRVCVGKSLARTELFLLFAGLL 454
Cdd:cd11027  318 TLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVpKPESFLPFSAGRRVCLGESLAKAELFLFLARLL 397
                        410
                 ....*....|....*.
gi 237681200 455 QRYRLLPPPGLSPADL 470
Cdd:cd11027  398 QKFRFSPPEGEPPPEL 413
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
66-474 3.21e-106

cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) consists of only one functional member CYP2B6, which shows broad substrate specificity and plays a key role in the metabolism of many clinical drugs, environmental toxins, and endogenous compounds. Rodents have multiple functional CYP2B proteins; mouse subfamily members include CYP2B9, 2B10, 2B13, 2B19, and 2B23. CYP2B enzymes are highly inducible by chemicals that interact with the constitutive androstane receptor (CAR) and/or pregnane X receptor (PXR), such as rifampicin and phenobarbital. The CYP2B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 322.88  E-value: 3.21e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFANGERWKTLRRFSLATMRDFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20672   81 VEERIQEEAQCLVEELRKSKGALLdPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 R-LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQE-DDPEDMFGEANVLACTLDMVMAGTE 302
Cdd:cd20672  161 GfLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEkSNHHTEFHHQNLMISVLSLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 303 TTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYL 381
Cdd:cd20672  241 TTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPiGVPHRVTKDTLFRGYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 382 LPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP 461
Cdd:cd20672  321 LPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVAS 400
                        410
                 ....*....|...
gi 237681200 462 PpgLSPADLDLRP 474
Cdd:cd20672  401 P--VAPEDIDLTP 411
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
67-483 4.79e-106

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 322.24  E-value: 4.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQqPSM 146
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKLK-KKM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 147 VGKVLQELACLKGQLDSYGGQPLPLAL---LGWAPCNITFTLLFGQRFD-YQDPVFVSLLSLIDQVMVLLGSPGIQLFNT 222
Cdd:cd20617   80 EELIEEEVNKLIESLKKHSKSGEPFDPrpyFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEEIFKELGSGNPSDFIP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPRLgaFLRLHRPVLSKI-EEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDmFGEANVLACTLDMVMAGT 301
Cdd:cd20617  160 ILLP--FYFLYLKKLKKSyDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGL-FDDDSIISTCLDLFLAGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 302 ETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGY 380
Cdd:cd20617  237 DTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPlGLPRVTTEDTEIGGY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRgAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLL 460
Cdd:cd20617  317 FIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSE-QFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFK 395
                        410       420
                 ....*....|....*....|...
gi 237681200 461 PPPGLspaDLDLRPAPAFTMRPP 483
Cdd:cd20617  396 SSDGL---PIDEKEVFGLTLKPK 415
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
66-487 3.08e-105

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 320.72  E-value: 3.08e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILRRFSLTILRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20670   81 IEERIQEEAGYLLEEFRKTKGAPIdPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLR-LHRPVLSKIEEVRTILRTLLETRRPPLPTGGPaQSYVEALLQQGQED--DPEDMFGEANVLACTLDMVMAGT 301
Cdd:cd20670  161 GIMQYLPgRHNRIYYLIEELKDFIASRVKINEASLDPQNP-RDFIDCFLIKMHQDknNPHTEFNLKNLVLTTLNLFFAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 302 ETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGY 380
Cdd:cd20670  240 ETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPlGVPHNVIRDTQFRGY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLL 460
Cdd:cd20670  320 LLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLR 399
                        410       420
                 ....*....|....*....|....*...
gi 237681200 461 PPpgLSPADLDLRPA-PAFTMRPPAQTL 487
Cdd:cd20670  400 SL--VPPADIDITPKiSGFGNIPPTYEL 425
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
66-487 1.35e-101

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 311.35  E-value: 1.35e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20668    1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRDFGVGKRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTF- 223
Cdd:cd20668   81 IEERIQEEAGFLIDALRGTGGAPIdPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFs 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 224 --------PRLGAFLRLHRPVLSKIEEVRTILRTLletrRPPLPtggpaQSYVEALLQQGQED--DPEDMFGEANVLACT 293
Cdd:cd20668  161 svmkhlpgPQQQAFKELQGLEDFIAKKVEHNQRTL----DPNSP-----RDFIDSFLIRMQEEkkNPNTEFYMKNLVMTT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTA 372
Cdd:cd20668  232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPmGLARRVT 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 373 ADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAG 452
Cdd:cd20668  312 KDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTT 391
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 237681200 453 LLQRYRLLPPpgLSPADLDLRPAP-AFTMRPPAQTL 487
Cdd:cd20668  392 IMQNFRFKSP--QSPEDIDVSPKHvGFATIPRNYTM 425
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
67-483 2.40e-99

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 305.30  E-value: 2.40e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALvgTGHELADRPPIPIFQHIQRGG--GIFFSSGARWRAGRQFTVRTLQSLGVQQP 144
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVREVL--SREEFDGRPDGFFFRLRTFGKrlGITFTDGPFWKEQRRFVLRHLRDFGFGRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 145 SMVGKVLQELACLKGQLDSYGGQPLPLALLgWAPC--NITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGiQLFNT 222
Cdd:cd20651   79 SMEEVIQEEAEELIDLLKKGEKGPIQMPDL-FNVSvlNVLWAMVAGERYSLEDQKLRKLLELVHLLFRNFDMSG-GLLNQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPrlgaFLRLHRPVLSK-------IEEVRTILRTLLETRRPPLPTGGPaQSYVEALLQQGQE-DDPEDMFGEANVLACTL 294
Cdd:cd20651  157 FP----WLRFIAPEFSGynllvelNQKLIEFLKEEIKEHKKTYDEDNP-RDLIDAYLREMKKkEPPSSSFTDDQLVMICL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAA 373
Cdd:cd20651  232 DLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPiGIPHRALK 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 374 DIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGL 453
Cdd:cd20651  312 DTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGL 391
                        410       420       430
                 ....*....|....*....|....*....|
gi 237681200 454 LQRYRLLPPPGLSPaDLDLRPAPAFTMRPP 483
Cdd:cd20651  392 LQNFTFSPPNGSLP-DLEGIPGGITLSPKP 420
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
66-473 3.76e-98

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 302.47  E-value: 3.76e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSS-GARWRAGRQFTVRTLQSLGVQQP 144
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPyGPVWRQQRKFSHSTLRHFGLGKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 145 SMVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVM-VLLGSPGIqLFNT 222
Cdd:cd20666   81 SLEPKIIEEFRYVKAEMLKHGGDPFnPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLeISVNSAAI-LVNI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPRLgaflrLHRPV-----LSKIE-EVRTILRTLLETRRPPLPTGGPaQSYVEALL---QQGQEDDPEDMFGEANVLACT 293
Cdd:cd20666  160 CPWL-----YYLPFgpfreLRQIEkDITAFLKKIIADHRETLDPANP-RDFIDMYLlhiEEEQKNNAESSFNEDYLFYII 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTA 372
Cdd:cd20666  234 GDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPlSIPHMAS 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 373 ADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAG 452
Cdd:cd20666  314 ENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVS 393
                        410       420
                 ....*....|....*....|.
gi 237681200 453 LLQRYRLLPPPGLSPADLDLR 473
Cdd:cd20666  394 LMQSFTFLLPPNAPKPSMEGR 414
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
66-476 1.18e-96

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 298.29  E-value: 1.18e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPS 145
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRELGLGKQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFP 224
Cdd:cd20667   81 LESQIQHEAAELVKVFAQENGRPFdPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLR-LHRPVLSKIEEVRTILRTllETRRPPLPTGGPAQSYVEALLQQ--GQEDDPEDMFGEANVLACTLDMVMAGT 301
Cdd:cd20667  161 WLMRYLPgPHQKIFAYHDAVRSFIKK--EVIRHELRTNEAPQDFIDCYLAQitKTKDDPVSTFSEENMIQVVIDLFLGGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 302 ETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGY 380
Cdd:cd20667  239 ETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSvGAVRQCVTSTTMHGY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLL 460
Cdd:cd20667  319 YVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQ 398
                        410       420
                 ....*....|....*....|..
gi 237681200 461 PPPGLSPADLD------LRPAP 476
Cdd:cd20667  399 LPEGVQELNLEyvfggtLQPQP 420
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
63-488 1.22e-94

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 293.64  E-value: 1.22e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  63 SERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGAR-WRAGRQFTVRTLQSLGV 141
Cdd:cd20661    9 SQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRgWTEHRKLAVNCFRYFGY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 142 QQPSMVGKVLQELACLKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLF 220
Cdd:cd20661   89 GQKSFESKISEECKFFLDAIDTYKGKPFdPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 221 NTFPRLGaFLRL--HRPVLSKIEEVRTILRTLL----ETRRPPLPtggpaQSYVEALLQQGQ--EDDPEDMFGEANVLAC 292
Cdd:cd20661  169 NAFPWIG-ILPFgkHQQLFRNAAEVYDFLLRLIerfsENRKPQSP-----RHFIDAYLDEMDqnKNDPESTFSMENLIFS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 293 TLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCT 371
Cdd:cd20661  243 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPlGIFHAT 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 372 AADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFA 451
Cdd:cd20661  323 SKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFT 402
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 237681200 452 GLLQRYRLLPPPGLSPadlDLRPAPAFTMRPPAQTLC 488
Cdd:cd20661  403 ALLQRFHLHFPHGLIP---DLKPKLGMTLQPQPYLIC 436
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
66-482 1.32e-82

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 262.23  E-value: 1.32e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSS-GARWRAGRQFTVRTLQSLGVQQP 144
Cdd:cd11028    1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSDyGPRWKLHRKLAQNALRTFSNART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 145 SMV--GKVLQELACLKGQLDSYGGQPLPL---ALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGI-- 217
Cdd:cd11028   81 HNPleEHVTEEAEELVTELTENNGKPGPFdprNEIYLSVGNVICAICFGKRYSRDDPEFLELVKSNDDFGAFVGAGNPvd 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 218 ---QLFNTFPR-LGAFLRLHRP----VLSKIEEvrtILRTLLETRRPPLptggpAQSYVEALLQQGQEDDPEDMFGEANV 289
Cdd:cd11028  161 vmpWLRYLTRRkLQKFKELLNRlnsfILKKVKE---HLDTYDKGHIRDI-----TDALIKASEEKPEEEKPEVGLTDEHI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 290 LACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVP 368
Cdd:cd11028  233 ISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPfTIP 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 369 RCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGA--FLPFSAGRRVCVGKSLARTEL 446
Cdd:cd11028  313 HATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTKVdkFLPFGAGRRRCLGEELARMEL 392
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 237681200 447 FLLFAGLLQRYRLLPPPGlspADLDLRPAPAFTMRP 482
Cdd:cd11028  393 FLFFATLLQQCEFSVKPG---EKLDLTPIYGLTMKP 425
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
66-481 4.03e-71

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 232.30  E-value: 4.03e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFfSSG---ARWRAGRQFTVRTLQsLGVQ 142
Cdd:cd20674    1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQDL-SLGdysLLWKAHRKLTRSALQ-LGIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 143 QpSMVGKVLQELACLKGQLDSYGGQPLPLAL-LGWAPCNITFTLLFGQRFDyQDPVFVSLLSLIDQVMVLLGSPGIQLFN 221
Cdd:cd20674   79 N-SLEPVVEQLTQELCERMRAQAGTPVDIQEeFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSIQALD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 222 TFPrlgaFLR-LHRPVLSK----IEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDM--FGEANVLACTL 294
Cdd:cd20674  157 SIP----FLRfFPNPGLRRlkqaVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEKGMgqLLEGHVHMAVV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAA 373
Cdd:cd20674  233 DLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPlALPHRTTR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 374 DIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGrfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGL 453
Cdd:cd20674  313 DSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGA---ANRALLPFGCGARVCLGEPLARLELFVFLARL 389
                        410       420       430
                 ....*....|....*....|....*....|....
gi 237681200 454 LQRYRLLPP-----PGLSP-ADLDLRPAPaFTMR 481
Cdd:cd20674  390 LQAFTLLPPsdgalPSLQPvAGINLKVQP-FQVR 422
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
67-484 1.44e-68

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 225.75  E-value: 1.44e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALvgTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLG-VQQPS 145
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDWLRQFGmTKFGN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 MVGKVLQELAC----LKGQLDSYGGQPL-PLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLF 220
Cdd:cd20652   79 GRAKMEKRIATgvheLIKHLKAESGQPVdPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLIGVAGPVNF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 221 NTFPR-LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPA------QSYVEALLQQGQEDDPEDMF-GEANVLAC 292
Cdd:cd20652  159 LPFLRhLPSYKKAIEFLVQGQAKTHAIYQKIIDEHKRRLKPENPRdaedfeLCELEKAKKEGEDRDLFDGFyTDEQLHHL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 293 TLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCT 371
Cdd:cd20652  239 LADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPlGIPHGC 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 372 AADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFA 451
Cdd:cd20652  319 TEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTA 398
                        410       420       430
                 ....*....|....*....|....*....|...
gi 237681200 452 GLLQRYRLLPPPGLsPADLdLRPAPAFTMRPPA 484
Cdd:cd20652  399 RILRKFRIALPDGQ-PVDS-EGGNVGITLTPPP 429
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
66-482 3.38e-68

cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410688 [Multi-domain]  Cd Length: 425  Bit Score: 224.76  E-value: 3.38e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFF--SSGARWRAGRqftvRTLQSLgvQQ 143
Cdd:cd11065    1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLlmPYGPRWRLHR----RLFHQL--LN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 144 PSMVGKV--LQEL---ACLKGQLDSyggqplPLALLGWA---PCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSP 215
Cdd:cd11065   75 PSAVRKYrpLQELeskQLLRDLLES------PDDFLDHIrryAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 216 GIQLFNTFPrlgaFLR-----LHRPVLSKIEEVRTILRTLLETR----RPPLPTGGPAQSYVEALLQQGQEDDPEDMFGE 286
Cdd:cd11065  149 GAYLVDFFP----FLRylpswLGAPWKRKARELRELTRRLYEGPfeaaKERMASGTATPSFVKDLLEELDKEGGLSEEEI 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 287 ANVLActlDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPH 366
Cdd:cd11065  225 KYLAG---SLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 367 -VPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLD---AKGRFMKRGAFlPFSAGRRVCVGKSLA 442
Cdd:cd11065  302 gIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDdpkGTPDPPDPPHF-AFGFGRRICPGRHLA 380
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 237681200 443 RTELFLLFAGLLQRYRLLPPPGLSPADLDLRPA--PAFTMRP 482
Cdd:cd11065  381 ENSLFIAIARLLWAFDIKKPKDEGGKEIPDEPEftDGLVSHP 422
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
66-482 4.60e-65

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 216.42  E-value: 4.60e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGG-GIFF-SSGARWRAGRQFTVRTLQSLGVQQ 143
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGkDIAFaDYSATWQLHRKLVHSAFALFGEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 144 PSMVGKVLQELACLKGQLDSYGGQPLPLAL-LGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGiqLFNT 222
Cdd:cd20673   81 QKLEKIICQEASSLCDTLATHNGESIDLSPpLFRAVTNVICLLCFNSSYKNGDPELETILNYNEGIVDTVAKDS--LVDI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPRLGAFLRLHRPVLSKIEEVR-TILRTLLETRRPPLpTGGPAQSYVEALLQ--------QGQEDDPEDMFGEANVLACT 293
Cdd:cd20673  159 FPWLQIFPNKDLEKLKQCVKIRdKLLQKKLEEHKEKF-SSDSIRDLLDALLQakmnaennNAGPDQDSVGLSDDHILMTV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRyI-----TLLPHVp 368
Cdd:cd20673  238 GDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLR-IrpvapLLIPHV- 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 369 rcTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMK--RGAFLPFSAGRRVCVGKSLARTEL 446
Cdd:cd20673  316 --ALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLIspSLSYLPFGAGPRVCLGEALARQEL 393
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 237681200 447 FLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRP 482
Cdd:cd20673  394 FLFMAWLLQRFDLEVPDGGQLPSLEGKFGVVLQIDP 429
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
66-454 8.86e-61

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 205.24  E-value: 8.86e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSS-GARWRAGR---QFTVRTL----- 136
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGySERWKAHRrvaHSTVRAFstrnp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 137 QSLGVQQPSMVGKVlQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQV--MVLLGS 214
Cdd:cd20675   81 RTRKAFERHVLGEA-RELVALFLRKSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLGRNDQFgrTVGAGS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 215 -----PGIQLFNTFPR--LGAFLRLHRpvlskiEEVRTILRTLLETRRPPlpTGGPAQSYVEAL---LQQGQEDDPEDMF 284
Cdd:cd20675  160 lvdvmPWLQYFPNPVRtvFRNFKQLNR------EFYNFVLDKVLQHRETL--RGGAPRDMMDAFilaLEKGKSGDSGVGL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 285 GEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLL 364
Cdd:cd20675  232 DKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 365 P-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAF--LPFSAGRRVCVGKSL 441
Cdd:cd20675  312 PvTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLASsvMIFSVGKRRCIGEEL 391
                        410
                 ....*....|...
gi 237681200 442 ARTELFLLFAGLL 454
Cdd:cd20675  392 SKMQLFLFTSILA 404
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
67-480 1.22e-60

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 203.90  E-value: 1.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQpsM 146
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAA--L 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 147 VGKVLQELACLKGQLDSYGGQPLPLALLGWA-PCNITFTLLFGQRFDYQDPVFVSLLSLIdqvmvllgspgIQLFNTFPR 225
Cdd:cd00302   79 RPVIREIARELLDRLAAGGEVGDDVADLAQPlALDVIARLLGGPDLGEDLEELAELLEAL-----------LKLLGPRLL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 226 LGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPaqSYVEALLQQGQEDDPEDMFGEANVlactldMVMAGTETTA 305
Cdd:cd00302  148 RPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLD--LLLLADADDGGGLSDEEIVAELLT------LLLAGHETTA 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 306 ATLQWAVFLMVKHPHVQGRVQEELDRVLGPgqlPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKG 385
Cdd:cd00302  220 SLLAWALYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAG 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 386 TPVIPLLTSVLLDKTQWETPSQFNPNHFLDakGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPgl 465
Cdd:cd00302  297 TLVLLSLYAAHRDPEVFPDPDEFDPERFLP--EREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVP-- 372
                        410
                 ....*....|....*
gi 237681200 466 sPADLDLRPAPAFTM 480
Cdd:cd00302  373 -DEELEWRPSLGTLG 386
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
66-482 1.79e-60

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 204.56  E-value: 1.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSS--GARWRAGRQFTVRTLQSLGVQQ 143
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEkyGESWKLHKKIAKNALRTFSKEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 144 PS------------------MVgKVLQELACLKGQLDsyggqplPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLI 205
Cdd:cd20677   81 AKsstcsclleehvcaeaseLV-KTLVELSKEKGSFD-------PVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEIN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 206 DQVMVLLGSPG----IQLFNTFP-----RLGAFL-RLHRPVLSKIEE---------VRTILRTLLetrrpplptggpaqs 266
Cdd:cd20677  153 NDLLKASGAGNladfIPILRYLPspslkALRKFIsRLNNFIAKSVQDhyatydknhIRDITDALI--------------- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 267 yveALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRA 346
Cdd:cd20677  218 ---ALCQERKAEDKSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKS 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 347 LPYTSAVLHEVQRYITLLPH-VPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGA 425
Cdd:cd20677  295 LHYTEAFINEVFRHSSFVPFtIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLV 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 237681200 426 --FLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGlspADLDLRPAPAFTMRP 482
Cdd:cd20677  375 ekVLIFGMGVRKCLGEDVARNEIFVFLTTILQQLKLEKPPG---QKLDLTPVYGLTMKP 430
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
67-482 6.52e-57

Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is considerably larger than in other taxa. In individual plant genomes, CYPs form the third largest family of plant genes; the two largest gene families code for F-box proteins and receptor-like kinases. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. However, there is a phenomenon called family creep, where a sequence (below 40% identity) is absorbed into a large family; this is seen in the plant CYP71 and CYP89 families. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP71 clan has expanded dramatically and represents 50% of all plant CYPs; it includes several families including CYP71, CYP73, CYP76, CYP81, CYP82, CYP89, and CYP93, among others. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 195.08  E-value: 6.52e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGG--IFFSSGARWRAGRQ------FTVRTLQS 138
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQdiVFAPYGPHWRHLRKictlelFSAKRLES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 139 L-GVQQpsmvgkvlQELACLKGQLDSYGGQPLPLAL---LGWAPCNITFTLLFGQRF----DYQDPVFVSLLSLIDQVMV 210
Cdd:cd20618   81 FqGVRK--------EELSHLVKSLLEESESGKPVNLrehLSDLTLNNITRMLFGKRYfgesEKESEEAREFKELIDEAFE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 211 LLGSPGIQLFNTFPR-------LGAFLRLHRPV---LSK-IEEVRtilrtllETRRPPLPTGGPAQSYVEALLQQGQEDD 279
Cdd:cd20618  153 LAGAFNIGDYIPWLRwldlqgyEKRMKKLHAKLdrfLQKiIEEHR-------EKRGESKKGGDDDDDLLLLLDLDGEGKL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 280 PEDmfgeaNVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQR 359
Cdd:cd20618  226 SDD-----NIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLR 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 360 Y---ITLLphVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKrGA---FLPFSAGR 433
Cdd:cd20618  301 LhppGPLL--LPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVK-GQdfeLLPFGSGR 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 237681200 434 RVCVGKSLARTELFLLFAGLLQRYRLLpPPGLSPADLDLRPAPAFTMRP 482
Cdd:cd20618  378 RMCPGMPLGLRMVQLTLANLLHGFDWS-LPGPKPEDIDMEEKFGLTVPR 425
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
66-483 1.44e-56

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 194.46  E-value: 1.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFS--SGARWRAGRQFTVRTLQSLGV-- 141
Cdd:cd20676    1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFStdSGPVWRARRKLAQNALKTFSIas 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 142 ---------------QQPSMVGKVLQELACLKGQLDSYGGQPLPLAllgwapcNITFTLLFGQRFDYQDPVFVSLLSLID 206
Cdd:cd20676   81 sptssssclleehvsKEAEYLVSKLQELMAEKGSFDPYRYIVVSVA-------NVICAMCFGKRYSHDDQELLSLVNLSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 207 QVMVLLGSPGIQLFntFPrlgaFLR-LHRPVLSKIEEVRTILRTLLetrrpplptggpaQSYVE---------------- 269
Cdd:cd20676  154 EFGEVAGSGNPADF--IP----ILRyLPNPAMKRFKDINKRFNSFL-------------QKIVKehyqtfdkdnirditd 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 270 ALLQQGQE----DDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQR 345
Cdd:cd20676  215 SLIEHCQDkkldENANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRP 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 346 ALPYTSAVLHEVQRYITLLPH-VPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRG 424
Cdd:cd20676  295 QLPYLEAFILETFRHSSFVPFtIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKT 374
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237681200 425 ---AFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLspaDLDLRPAPAFTMRPP 483
Cdd:cd20676  375 eseKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPGV---KVDMTPEYGLTMKHK 433
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
63-491 7.51e-55

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 189.67  E-value: 7.51e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  63 SERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPP---IPIFQHIqrGGGIFF-SSGARWRAGRQ------FT 132
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVpdaVRALGHH--KSSIVWpPYGPRWRMLRKicttelFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 133 VRTLQSlgvQQPSMVGKVLQELACLKGQLDSYG----GQPLPLALLgwapcNITFTLLFGQR-FDYQDPVFVSLLSLIDQ 207
Cdd:cd11073   79 PKRLDA---TQPLRRRKVRELVRYVREKAGSGEavdiGRAAFLTSL-----NLISNTLFSVDlVDPDSESGSEFKELVRE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 208 VMVLLGSPGIQLFntFPRLGAF----LRlhRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDM 283
Cdd:cd11073  151 IMELAGKPNVADF--FPFLKFLdlqgLR--RRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSESE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 284 FGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRY--- 360
Cdd:cd11073  227 LTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLhpp 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 361 ITLLphVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFmkRGA---FLPFSAGRRVCV 437
Cdd:cd11073  307 APLL--LPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDF--KGRdfeLIPFGSGRRICP 382
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 237681200 438 GKSLA-RTELFLLfAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRpPAQTLCVVP 491
Cdd:cd11073  383 GLPLAeRMVHLVL-ASLLHSFDWKLPDGMKPEDLDMEEKFGLTLQ-KAVPLKAIP 435
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
65-483 2.18e-49

cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 175.12  E-value: 2.18e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  65 RYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPP-IPIFQHIQRGG-GIFFSS-GARWRAGRqftvRTLQSlGV 141
Cdd:cd11075    1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPaNPLRVLFSSNKhMVNSSPyGPLWRTLR----RNLVS-EV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 142 QQPSMVGK-------VLQELacLKGQLDSYGGQPLPLALLGwapcNITFTLL-------FGQRFDyqDPVFVSLLSLIDQ 207
Cdd:cd11075   76 LSPSRLKQfrparrrALDNL--VERLREEAKENPGPVNVRD----HFRHALFslllymcFGERLD--EETVRELERVQRE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 208 VMVLLGSPgiQLFNTFPRLGAFLRlhRPVLSKIEEVRT----ILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEdm 283
Cdd:cd11075  148 LLLSFTDF--DVRDFFPALTWLLN--RRRWKKVLELRRrqeeVLLPLIRARRKRRASGEADKDYTDFLLLDLLDLKEE-- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 284 fGEANVLA----CTL--DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHE- 356
Cdd:cd11075  222 -GGERKLTdeelVSLcsEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLEt 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 357 VQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKG--------RFMKrgaFLP 428
Cdd:cd11075  301 LRRHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEaadidtgsKEIK---MMP 377
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 237681200 429 FSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGlspADLDLRPAPAFT--MRPP 483
Cdd:cd11075  378 FGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEG---EEVDFSEKQEFTvvMKNP 431
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
35-470 5.55e-49

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 175.69  E-value: 5.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  35 PPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQhIQRG 114
Cdd:PLN02394  32 PPGPAAVPIFGNWLQVGDDLNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD-IFTG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 115 GG---IFFSSGARWRAGRQ------FTVRTLQSLGVQQPSMVGKVLQELaclKGQLDSYGG-----QPLPLALLgwapcN 180
Cdd:PLN02394 111 KGqdmVFTVYGDHWRKMRRimtvpfFTNKVVQQYRYGWEEEADLVVEDV---RANPEAATEgvvirRRLQLMMY-----N 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 181 ITFTLLFGQRFDYQ-DPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHrpvLSKIEEVRTILRTL-----LETR 254
Cdd:PLN02394 183 IMYRMMFDRRFESEdDPLFLKLKALNGERSRLAQSFEYNYGDFIPILRPFLRGY---LKICQDVKERRLALfkdyfVDER 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 255 RPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLG 334
Cdd:PLN02394 260 KKLMSAKGMDKEGLKCAIDHILEAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLG 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 335 PG-QLPQPEHQRaLPYTSAVLHEVQRY---ITLLphVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNP 410
Cdd:PLN02394 340 PGnQVTEPDTHK-LPYLQAVVKETLRLhmaIPLL--VPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRP 416
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237681200 411 NHFLDAKGRFMKRGA---FLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADL 470
Cdd:PLN02394 417 ERFLEEEAKVEANGNdfrFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQSKIDV 479
PTZ00404 PTZ00404
cytochrome P450; Provisional
36-459 2.67e-48

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 173.37  E-value: 2.67e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  36 PGPRPLPFLGNLHLLGvTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGG 115
Cdd:PTZ00404  32 KGPIPIPILGNLHQLG-NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 116 GIFFSSGARWRAGRQFTVRTLQSLGVQQP-SMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQ 194
Cdd:PTZ00404 111 GIVTSSGEYWKRNREIVGKAMRKTNLKHIyDLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFKYIFNEDISFD 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 195 DPVFVSLLSLIDQVMVllgspgiQLFNTFPR--LGAFLRLHRPV----LSKIEEVRTILRTL--------LETRRPPLPt 260
Cdd:PTZ00404 191 EDIHNGKLAELMGPME-------QVFKDLGSgsLFDVIEITQPLyyqyLEHTDKNFKKIKKFikekyhehLKTIDPEVP- 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 261 ggpaQSYVEALLQQGQEDDPEDMFgeaNVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQ 340
Cdd:PTZ00404 263 ----RDLLDLLIKEYGTNTDDDIL---SILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVL 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 341 PEHQRALPYTSAVLHEVQRYITLLPH-VPRCTAADIQLG-GYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKG 418
Cdd:PTZ00404 336 LSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGgGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDS 415
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 237681200 419 RFmkrgAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRL 459
Cdd:PTZ00404 416 ND----AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKL 452
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
65-481 1.89e-47

cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 169.57  E-value: 1.89e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  65 RYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGG-GIFFSS-GARWRAGRQFTVRTLQSlgvq 142
Cdd:cd11072    1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGkDIAFAPyGEYWRQMRKICVLELLS---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 143 qPSMV---GKVLQ-ELACLKGQLDSYGGQPLPL---ALLGWAPCNITFTLLFGQRFDYQDPVfvSLLSLIDQVMVLLGSP 215
Cdd:cd11072   77 -AKRVqsfRSIREeEVSLLVKKIRESASSSSPVnlsELLFSLTNDIVCRAAFGRKYEGKDQD--KFKELVKEALELLGGF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 216 GIQLFntFPRLGaFLRLHRPVLSKIEEVRTILRTLLET-----RRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVL 290
Cdd:cd11072  154 SVGDY--FPSLG-WIDLLTGLDRKLEKVFKELDAFLEKiidehLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNIK 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 291 ACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRY---ITLLphV 367
Cdd:cd11072  231 AIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLhppAPLL--L 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 368 PRCTAADIQLGGYLLPKGTPVI---------PLLtsvlldktqWETPSQFNPNHFLDAKGRFmkRGA---FLPFSAGRRV 435
Cdd:cd11072  309 PRECREDCKINGYDIPAKTRVIvnawaigrdPKY---------WEDPEEFRPERFLDSSIDF--KGQdfeLIPFGAGRRI 377
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 237681200 436 CVGKSLART--ELFLlfAGLLQRY--RLlpPPGLSPADLDLRPAPAFTMR 481
Cdd:cd11072  378 CPGITFGLAnvELAL--ANLLYHFdwKL--PDGMKPEDLDMEEAFGLTVH 423
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
66-485 3.34e-47

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 169.20  E-value: 3.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGG--IFFSSGARWRAGRQ------FTVRTLQ 137
Cdd:cd20656    1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQdlIWADYGPHYVKVRKlctlelFTPKRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 138 SL----GVQQPSMVGKVLQELAclkgqLDSYGGQPLPLA--LLGWAPCNITfTLLFGQRF----DYQDPVFVSLLSLIDQ 207
Cdd:cd20656   81 SLrpirEDEVTAMVESIFNDCM-----SPENEGKPVVLRkyLSAVAFNNIT-RLAFGKRFvnaeGVMDEQGVEFKAIVSN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 208 VMVLLGSpgIQLFNTFPRLGAFLRLHRPVLSKIEEVRTIL-RTLLETRRPPLPTGGPAQSYVEALLQQGQEDDpedmFGE 286
Cdd:cd20656  155 GLKLGAS--LTMAEHIPWLRWMFPLSEKAFAKHGARRDRLtKAIMEEHTLARQKSGGGQQHFVALLTLKEQYD----LSE 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 287 ANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRY----IT 362
Cdd:cd20656  229 DTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLhpptPL 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 363 LLPHVprcTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL----DAKGRFMKrgaFLPFSAGRRVCVG 438
Cdd:cd20656  309 MLPHK---ASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLeedvDIKGHDFR---LLPFGAGRRVCPG 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 237681200 439 KSLARTELFLLFAGLLQRYRLLPPPGLSPADLDL--RPAPAFTMRPPAQ 485
Cdd:cd20656  383 AQLGINLVTLMLGHLLHHFSWTPPEGTPPEEIDMteNPGLVTFMRTPLQ 431
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
296-482 2.55e-44

cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of Mycobacterium tuberculosis cytochrome P450 132 (CYP132) and similar proteins. The function of CYP132 is as yet unknown. CYP132 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410713 [Multi-domain]  Cd Length: 406  Bit Score: 160.82  E-value: 2.55e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 296 MVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRyitLLPHV---PRCTA 372
Cdd:cd20620  220 LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLR---LYPPAwiiGREAV 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 373 ADIQLGGYLLPKGTPVI--PLLTSvlLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLF 450
Cdd:cd20620  296 EDDEIGGYRIPAGSTVLisPYVTH--RDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLL 373
                        170       180       190
                 ....*....|....*....|....*....|..
gi 237681200 451 AGLLQRYRLLPPPGLSPadldlRPAPAFTMRP 482
Cdd:cd20620  374 ATIAQRFRLRLVPGQPV-----EPEPLITLRP 400
PLN02687 PLN02687
flavonoid 3'-monooxygenase
35-492 9.47e-44

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 161.52  E-value: 9.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  35 PPGPRPLPFLGNLHLLGvTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRG 114
Cdd:PLN02687  36 PPGPRGWPVLGNLPQLG-PKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 115 GG--IFFSSGARWRAGRQ------FTVRTLQSL-GVQQpsmvgkvlQELACLKGQLDSYGGQ-PLPLA-LLGWAPCNITF 183
Cdd:PLN02687 115 YQdlVFAPYGPRWRALRKicavhlFSAKALDDFrHVRE--------EEVALLVRELARQHGTaPVNLGqLVNVCTTNALG 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 184 TLLFGQRF--DYQDPVFVSLLSLIDQVMVLLGS-------PGIQLFNTFPRLGAFLRLHR---PVLSKIEEVRTIlrtll 251
Cdd:PLN02687 187 RAMVGRRVfaGDGDEKAREFKEMVVELMQLAGVfnvgdfvPALRWLDLQGVVGKMKRLHRrfdAMMNGIIEEHKA----- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 252 eTRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDR 331
Cdd:PLN02687 262 -AGQTGSEEHKDLLSTLLALKREQQADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDA 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 332 VLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNP 410
Cdd:PLN02687 341 VVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPlSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRP 420
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 411 NHFL--------DAKGRFMKrgaFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRp 482
Cdd:PLN02687 421 DRFLpggehagvDVKGSDFE---LIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTPDKLNMEEAYGLTLQ- 496
                        490
                 ....*....|
gi 237681200 483 PAQTLCVVPR 492
Cdd:PLN02687 497 RAVPLMVHPR 506
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
57-483 1.87e-42

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 155.82  E-value: 1.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  57 RALMELSERYGPMFTIHLGSQK-TVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQ----- 130
Cdd:cd11053    2 GFLERLRARYGDVFTLRVPGLGpVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLLLLDGDRHRRRRKllmpa 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 131 FTVRTLQSLGVQQPSMVGKVLQELAclKGQldsyggqplPLALLGWAPcNITF----TLLFGQrfdYQDPVFVSLLSLID 206
Cdd:cd11053   82 FHGERLRAYGELIAEITEREIDRWP--PGQ---------PFDLRELMQ-EITLevilRVVFGV---DDGERLQELRRLLP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 207 QVMVLLGSPGIQLFNTFPRLGAFLRLHRpVLSKIEEVRTILRTLLETRRP-PLPTGgpaqSYVEALLQQGQEDDPEDMfG 285
Cdd:cd11053  147 RLLDLLSSPLASFPALQRDLGPWSPWGR-FLRARRRIDALIYAEIAERRAePDAER----DDILSLLLSARDEDGQPL-S 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 286 EANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPgqlPQPEHQRALPYTSAVLHEVQRYITLLP 365
Cdd:cd11053  221 DEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGD---PDPEDIAKLPYLDAVIKETLRLYPVAP 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 366 HVPRCTAADIQLGGYLLPKGTPVIPlltSVLL---DKTQWETPSQFNPNHFLDAKgrfMKRGAFLPFSAGRRVCVGKSLA 442
Cdd:cd11053  298 LVPRRVKEPVELGGYTLPAGTTVAP---SIYLthhRPDLYPDPERFRPERFLGRK---PSPYEYLPFGGGVRRCIGAAFA 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 237681200 443 RTELFLLFAGLLQRYRLLPPPGlspadldlRPAPA----FTMRPP 483
Cdd:cd11053  372 LLEMKVVLATLLRRFRLELTDP--------RPERPvrrgVTLAPS 408
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
25-484 3.71e-42

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 154.67  E-value: 3.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  25 TRSPSLAPRWPPGPR----PLPFLGNLHllgvtqqdralmelseRYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELA 100
Cdd:COG2124    2 TATATPAADLPLDPAflrdPYPFYARLR----------------EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 101 DRPPIPIFQHIQR-GGGIFFSSGARWRAGRQ-----FTVRTLQSLGvqqPSMVGKVLQELACL--KGQLDSYG--GQPLP 170
Cdd:COG2124   66 DGGLPEVLRPLPLlGDSLLTLDGPEHTRLRRlvqpaFTPRRVAALR---PRIREIADELLDRLaaRGPVDLVEefARPLP 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 171 LallgwapcnITFTLLFGQRFDYQDPvfvsLLSLIDQVMVLLGSPgiqlfnTFPRLGAFLRLHRpvlskieEVRTILRTL 250
Cdd:COG2124  143 V---------IVICELLGVPEEDRDR----LRRWSDALLDALGPL------PPERRRRARRARA-------ELDAYLREL 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 251 LETRRpplptGGPAQSYVEALLQqgQEDDPEDMfGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEld 330
Cdd:COG2124  197 IAERR-----AEPGDDLLSALLA--ARDDGERL-SDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-- 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 331 rvlgpgqlpqpehqraLPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNP 410
Cdd:COG2124  267 ----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDP 330
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237681200 411 nhfldakGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYrllppPGLSPA-DLDLRPAPAFTMRPPA 484
Cdd:COG2124  331 -------DR--PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRF-----PDLRLApPEELRWRPSLTLRGPK 391
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
33-492 6.32e-42

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 156.52  E-value: 6.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  33 RWPPGPRPLPFLGNLHLLGvTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQ 112
Cdd:PLN03112  32 RLPPGPPRWPIVGNLLQLG-PLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 113 RGGGIFFSS--GARWRAGRQFTVRTLQSLGvQQPSMVGKVLQELACLKGQL--DSYGGQPLPL--ALLGWAPCNITFTLL 186
Cdd:PLN03112 111 YGCGDVALAplGPHWKRMRRICMEHLLTTK-RLESFAKHRAEEARHLIQDVweAAQTGKPVNLreVLGAFSMNNVTRMLL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 187 FGQRFDYQDPVF---VSLLSLIDQVMVLLGSpgIQLFNTFPRLG-----AFLRLHRPVLSKIEEVRT-ILRTLLETRRPP 257
Cdd:PLN03112 190 GKQYFGAESAGPkeaMEFMHITHELFRLLGV--IYLGDYLPAWRwldpyGCEKKMREVEKRVDEFHDkIIDEHRRARSGK 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 258 LPTGGPaQSYVEALLQQGQEDDPEDMfGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQ 337
Cdd:PLN03112 268 LPGGKD-MDFVDVLLSLPGENGKEHM-DDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNR 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 338 LPQPEHQRALPYTSAVLHEVQRYITLLPH-VPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPN-HFLD 415
Cdd:PLN03112 346 MVQESDLVHLNYLRCVVRETFRMHPAGPFlIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPErHWPA 425
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 416 AKGRF-MKRGA---FLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMrPPAQTLCVV- 490
Cdd:PLN03112 426 EGSRVeISHGPdfkILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRPEDIDTQEVYGMTM-PKAKPLRAVa 504

                 ...
gi 237681200 491 -PR 492
Cdd:PLN03112 505 tPR 507
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
64-471 6.75e-42

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 154.94  E-value: 6.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  64 ERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQhIQRGGG---IFFSSGARWRAGRQ------FTVR 134
Cdd:cd11074    1 KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD-IFTGKGqdmVFTVYGEHWRKMRRimtvpfFTNK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 135 TLQSLGVQQPSMVGKVLQELacLKGQLDSYGGQPLP--LALLGWapcNITFTLLFGQRFDYQ-DPVFVSLLSLIDQVMVL 211
Cdd:cd11074   80 VVQQYRYGWEEEAARVVEDV--KKNPEAATEGIVIRrrLQLMMY---NNMYRIMFDRRFESEdDPLFVKLKALNGERSRL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 212 LGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVRTIL--RTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANV 289
Cdd:cd11074  155 AQSFEYNYGDFIPILRPFLRGYLKICKEVKERRLQLfkDYFVDERKKLGSTKSTKNEGLKCAIDHILDAQKKGEINEDNV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 290 LACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPG-QLPQPEHQRaLPYTSAVLHEVQRYITLLP-HV 367
Cdd:cd11074  235 LYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGvQITEPDLHK-LPYLQAVVKETLRLRMAIPlLV 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 368 PRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGA---FLPFSAGRRVCVGKSLART 444
Cdd:cd11074  314 PHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEANGNdfrYLPFGVGRRSCPGIILALP 393
                        410       420
                 ....*....|....*....|....*..
gi 237681200 445 ELFLLFAGLLQRYRLLPPPGLSPADLD 471
Cdd:cd11074  394 ILGITIGRLVQNFELLPPPGQSKIDTS 420
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
67-482 8.53e-42

unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 154.02  E-value: 8.53e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALVGTGHELA-DRPPIPIFQHIqRGGGIFFSSGARWRAGRQ-----FTVRTLQSLG 140
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRrISSLESVFREM-GINGVFSAEGDAWRRQRRlvmpaFSPKHLRYFF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 141 VQQPSMVGKVLQELACLKGQldsygGQPLPL-ALLGWAPCNITFTLLFGQRFDyqdpvfvsllsLIDQvmvllGSPGIQ- 218
Cdd:cd11083   80 PTLRQITERLRERWERAAAE-----GEAVDVhKDLMRYTVDVTTSLAFGYDLN-----------TLER-----GGDPLQe 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 219 -LFNTFP----RLGA------FLRL--HRPVLSKIEEVRTILRTLLETRRPPL---PTGGPAQSYVEALLQQgqEDDPED 282
Cdd:cd11083  139 hLERVFPmlnrRVNApfpywrYLRLpaDRALDRALVEVRALVLDIIAAARARLaanPALAEAPETLLAMMLA--EDDPDA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 283 MFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQ-RALPYTSAVLHEVQRYI 361
Cdd:cd11083  217 RLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEAlDRLPYLEAVARETLRLK 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 362 TLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLD--AKGRFMKRGAFLPFSAGRRVCVGK 439
Cdd:cd11083  297 PVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDgaRAAEPHDPSSLLPFGAGPRLCPGR 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 237681200 440 SLARTELFLLFAGLLQRYRL-LPPPGLSPADLdlrpaPAFTMRP 482
Cdd:cd11083  377 SLALMEMKLVFAMLCRNFDIeLPEPAPAVGEE-----FAFTMSP 415
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
64-459 1.13e-41

cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 153.84  E-value: 1.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  64 ERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGhELADRPPIPIFQHI----QRGGGIFFSSGARWRagrqfTVRTLqsl 139
Cdd:cd11054    2 KKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEG-KYPIRPSLEPLEKYrkkrGKPLGLLNSNGEEWH-----RLRSA--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 140 gVQQPSMVGKV-------LQELAC-----LKGQLDSYGGQP--LPLALLGWApcnI--TFTLLFGQRFDYQDPVFVSLLS 203
Cdd:cd11054   73 -VQKPLLRPKSvasylpaINEVADdfverIRRLRDEDGEEVpdLEDELYKWS---LesIGTVLFGKRLGCLDDNPDSDAQ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 204 -LIDQVMvllgspgiQLFNTFPRLGAFLRLHRPVLSK------------IEEVRTILRTLLETRRPPLPTGGPAQSYVEA 270
Cdd:cd11054  149 kLIEAVK--------DIFESSAKLMFGPPLWKYFPTPawkkfvkawdtiFDIASKYVDEALEELKKKDEEDEEEDSLLEY 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 271 LLQQGqEDDPEDmfgeanVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYT 350
Cdd:cd11054  221 LLSKP-GLSKKE------IVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 351 SAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAF--LP 428
Cdd:cd11054  294 KACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNIHPFasLP 373
                        410       420       430
                 ....*....|....*....|....*....|.
gi 237681200 429 FSAGRRVCVGKSLARTELFLLFAGLLQRYRL 459
Cdd:cd11054  374 FGFGPRMCIGRRFAELEMYLLLAKLLQNFKV 404
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
33-472 7.40e-41

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 153.31  E-value: 7.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  33 RWPPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQ 112
Cdd:PLN03234  28 RLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 113 RGGGI--FFSSGARWRAGRQFTVRTLQSlgvqqPSMVG--KVLQELACLK------GQLDSYGGQPLPLALLGWAPCnIT 182
Cdd:PLN03234 108 YQGRElgFGQYTAYYREMRKMCMVNLFS-----PNRVAsfRPVREEECQRmmdkiyKAADQSGTVDLSELLLSFTNC-VV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 183 FTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQ-LFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTG 261
Cdd:PLN03234 182 CRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSdLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDETLDPNRPK 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 262 GPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQP 341
Cdd:PLN03234 262 QETESFIDLLMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSE 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 342 EHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDA-KG 418
Cdd:PLN03234 342 EDIPNLPYLKAVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMKEhKG 421
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 237681200 419 RFMKRGAF--LPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDL 472
Cdd:PLN03234 422 VDFKGQDFelLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPEDIKM 477
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
67-480 2.70e-40

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 150.46  E-value: 2.70e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIqrggGIFFSS------GARWRAGRQ------FTVR 134
Cdd:cd20654    1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLM----GYNYAMfgfapyGPYWRELRKiatlelLSNR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 135 TLQSLGVQQPSMVGKVLQEL-ACLKGQLDSYGGQPLPLA-LLGWAPCNITFTLLFGQRF-----DYQDPVFVSLLSLIDQ 207
Cdd:cd20654   77 RLEKLKHVRVSEVDTSIKELySLWSNNKKGGGGVLVEMKqWFADLTFNVILRMVVGKRYfggtaVEDDEEAERYKKAIRE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 208 VMVLLGSpgIQLFNTFPRLG--AFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQS-----YVEALLQQGQE--- 277
Cdd:cd20654  157 FMRLAGT--FVVSDAIPFLGwlDFGGHEKAMKRTAKELDSILEEWLEEHRQKRSSSGKSKNdedddDVMMLSILEDSqis 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 278 -DDPeDMFGEANVLactlDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHE 356
Cdd:cd20654  235 gYDA-DTVIKATCL----ELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 357 VQR-YITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL------DAKGRFMKrgaFLPF 429
Cdd:cd20654  310 TLRlYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLtthkdiDVRGQNFE---LIPF 386
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 237681200 430 SAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPpglSPADLDLRPAPAFTM 480
Cdd:cd20654  387 GSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTP---SNEPVDMTEGPGLTN 434
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
231-482 4.49e-39

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 146.63  E-value: 4.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 231 RLHRPvlskIEEVRTILRTLLETRRpplpTGGPAQSYVEALLQQGQEDDPEDMfGEANVLACTLDMVMAGTETTAATLQW 310
Cdd:cd11049  172 RFDRA----LARLRELVDEIIAEYR----ASGTDRDDLLSLLLAARDEEGRPL-SDEELRDQVITLLTAGTETTASTLAW 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 311 AVFLMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIP 390
Cdd:cd11049  243 AFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAF 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 391 LLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPadl 470
Cdd:cd11049  322 SPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPV--- 398
                        250
                 ....*....|..
gi 237681200 471 dlRPAPAFTMRP 482
Cdd:cd11049  399 --RPRPLATLRP 408
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
57-471 2.94e-38

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 144.78  E-value: 2.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  57 RALMELSerygpmftihLGSQKTVVLSGYEVVREALVGTGheLADRPPIPIFQHIQRGGGI-FFSSGARWRAGRQ----- 130
Cdd:cd11076    3 KRLMAFS----------LGETRVVITSHPETAREILNSPA--FADRPVKESAYELMFNRAIgFAPYGEYWRNLRRiasnh 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 131 -FTVRTLQSLGvqqPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNItFTLLFGQRFDYQDPVFVS--LLSLIDQ 207
Cdd:cd11076   71 lFSPRRIAASE---PQRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLNNI-MGSVFGRRYDFEAGNEEAeeLGEMVRE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 208 VMVLLGspgiqLFN---TFPRLGAF--LRLHRPVLSKIEEVRTILRTLL-ETRRPPLPTGGPAQSYVEALLQ-QGqeddp 280
Cdd:cd11076  147 GYELLG-----AFNwsdHLPWLRWLdlQGIRRRCSALVPRVNTFVGKIIeEHRAKRSNRARDDEDDVDVLLSlQG----- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 281 EDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRY 360
Cdd:cd11076  217 EEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 361 itllpHVP-------RCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGR--FMKRGAFL---P 428
Cdd:cd11076  297 -----HPPgpllswaRLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGadVSVLGSDLrlaP 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 237681200 429 FSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGlSPADLD 471
Cdd:cd11076  372 FGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDA-KPVDLS 413
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
273-482 2.19e-37

cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the omega-hydroxylation of the terminal carbon of fatty acids, including essential signaling molecules such as eicosanoids, prostaglandins and leukotrienes, and they are important for chemical defense. There are seven vertebrate family 4 subfamilies: CYP4A, CYP4B, CYP4F, CYP4T, CYP4V, CYP4X, and CYP4Z; three (CYP4X, CYP4A, CYP4Z) are specific to mammals. CYP4 enzymes metabolize fatty acids off various length, level of saturation, and branching. Specific subfamilies show preferences for the length of fatty acids; CYP4B, CYP4A and CYP4V, and CYP4F preferentially metabolize short (C7-C10), medium (C10-C16), and long to very long (C18-C26) fatty acid chains, respectively. CYP4 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410721 [Multi-domain]  Cd Length: 426  Bit Score: 142.28  E-value: 2.19e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 273 QQGQEDDPEDMFGEANvlacTldMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGP-GQLPQPEHQRALPYTS 351
Cdd:cd20628  220 EDGGPLTDEDIREEVD----T--FMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDdDRRPTLEDLNKMKYLE 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 352 AVLHEVQRyitLLPHVP---RCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLP 428
Cdd:cd20628  294 RVIKETLR---LYPSVPfigRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIP 370
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 237681200 429 FSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPglsPADlDLRPAPAFTMRP 482
Cdd:cd20628  371 FSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVP---PGE-DLKLIAEIVLRS 420
PLN00168 PLN00168
Cytochrome P450; Provisional
33-464 1.31e-36

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 141.63  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  33 RWPPGPRPLPFLGNLHLLGVTQQD--RALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQH 110
Cdd:PLN00168  35 RLPPGPPAVPLLGSLVWLTNSSADvePLLRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 111 IQRGGGIFFSS--GARWRAGRQ-FTVRTLQSLGVQQPSMV-GKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLL 186
Cdd:PLN00168 115 LGESDNTITRSsyGPVWRLLRRnLVAETLHPSRVRLFAPArAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMC 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 187 FGQRFDYQDpvfVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAflRLHRPVLSKIEEVRTILRTLL--------ETRRPPL 258
Cdd:PLN00168 195 FGERLDEPA---VRAIAAAQRDWLLYVSKKMSVFAFFPAVTK--HLFRGRLQKALALRRRQKELFvplidarrEYKNHLG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 259 PTGGPAQ-------SYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDR 331
Cdd:PLN00168 270 QGGEPPKkettfehSYVDTLLDIRLPEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKA 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 332 VLGPGQLPQPEHQ-RALPYTSAVLHEVQRYIT----LLPHVPrctAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPS 406
Cdd:PLN00168 350 KTGDDQEEVSEEDvHKMPYLKAVVLEGLRKHPpahfVLPHKA---AEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPM 426
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237681200 407 QFNPNHFL---DAKGRFM---KRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPG 464
Cdd:PLN00168 427 EFVPERFLaggDGEGVDVtgsREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFEWKEVPG 490
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
299-482 1.32e-35

cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is composed of family 4 cytochrome P450s from vertebrate subfamilies A (CYP4A), B (CYP4B), F (CYP4F), T (CYP4T), X (CYP4X), and Z (CYP4Z). Also included are similar proteins from lancelets, tunicates, hemichordates, echinoderms, mollusks, annelid worms, sponges, and choanoflagellates, among others. The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B and CYP4F are conserved among vertebrates. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4F enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4B_4F-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 137.30  E-value: 1.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 299 AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLG 378
Cdd:cd20659  238 AGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITID 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 379 GYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYR 458
Cdd:cd20659  318 GVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFE 397
                        170       180
                 ....*....|....*....|....
gi 237681200 459 LLPPPglspaDLDLRPAPAFTMRP 482
Cdd:cd20659  398 LSVDP-----NHPVEPKPGLVLRS 416
PLN02183 PLN02183
ferulate 5-hydroxylase
32-492 2.41e-35

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 138.06  E-value: 2.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  32 PRWPPGPRPLPFLGNLHLLGVTQQdRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPP-IPI-FQ 109
Cdd:PLN02183  35 LPYPPGPKGLPIIGNMLMMDQLTH-RGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPAnIAIsYL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 110 HIQRGGGIFFSSGARWRAGRQFTVRTLQSLgvQQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWA-PCNITFTLLFG 188
Cdd:PLN02183 114 TYDRADMAFAHYGPFWRQMRKLCVMKLFSR--KRAESWASVRDEVDSMVRSVSSNIGKPVNIGELIFTlTRNITYRAAFG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 189 QRFDYQDPVFVSLLSLIDQvmvLLGSPGIQLFntFPRLG--------AFLRLHRPVLSKIeeVRTILRTLLETRR--PPL 258
Cdd:PLN02183 192 SSSNEGQDEFIKILQEFSK---LFGAFNVADF--IPWLGwidpqglnKRLVKARKSLDGF--IDDIIDDHIQKRKnqNAD 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 259 PTGGPAQS-YVEALL----QQGQEDDPEDM-----FGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEE 328
Cdd:PLN02183 265 NDSEEAETdMVDDLLafysEEAKVNESDDLqnsikLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQE 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 329 LDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQF 408
Cdd:PLN02183 345 LADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTF 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 409 NPNHFLDAKGRFMKRG--AFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMrPPAQT 486
Cdd:PLN02183 425 KPSRFLKPGVPDFKGShfEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELPDGMKPSELDMNDVFGLTA-PRATR 503

                 ....*.
gi 237681200 487 LCVVPR 492
Cdd:PLN02183 504 LVAVPT 509
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
186-473 5.37e-35

cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces cerevisiae cytochrome P450 56, also called cytochrome P450-DIT2, and similar fungal proteins. CYP56 is involved in spore wall maturation and is thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine-containing precursors of the spore wall. The CYP56-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 135.92  E-value: 5.37e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 186 LFGQRFDYQDPVFVSLLSLIDQVMVLLGSPgiqLFNTFPRLGAFLRLHRP-VLSKIEEVRTILRTLLETRR---PPLPTG 261
Cdd:cd11070  122 GFGFDLPALDEEESSLHDTLNAIKLAIFPP---LFLNFPFLDRLPWVLFPsRKRAFKDVDEFLSELLDEVEaelSADSKG 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 262 GPAQSYVEALLQQGQEDDP----EDMFGEANVlactldMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQ 337
Cdd:cd11070  199 KQGTESVVASRLKRARRSGglteKELLGNLFI------FFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEP 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 338 LPQPEHQ--RALPYTSAVLHEVQRYITLLPHVPRCTAADIQL-----GGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFN 409
Cdd:cd11070  273 DDWDYEEdfPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFD 352
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 410 PNHFLD------AKGRFMK-RGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPP------------GLSPADL 470
Cdd:cd11070  353 PERWGStsgeigAATRFTPaRGAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRVDPeweegetpagatRDSPAKL 432

                 ...
gi 237681200 471 DLR 473
Cdd:cd11070  433 RLR 435
PLN02966 PLN02966
cytochrome P450 83A1
33-491 1.10e-34

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 136.03  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  33 RWPPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPipifqhiq 112
Cdd:PLN02966  29 KLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPP-------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 113 RGGGIFFSSGARWRAGRQFT--VRTLQSLGVQQ---PSMVGK---VLQELAclKGQLDSYGGQPLPLALLGWAPCNITFT 184
Cdd:PLN02966 101 HRGHEFISYGRRDMALNHYTpyYREIRKMGMNHlfsPTRVATfkhVREEEA--RRMMDKINKAADKSEVVDISELMLTFT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 185 ------LLFGQRFDYQDPVFVSLLSLIDQVMVLLGS-------PGIQLFNTFPRLGAFLRlhrpvlSKIEEVRTILRTLL 251
Cdd:PLN02966 179 nsvvcrQAFGKKYNEDGEEMKRFIKILYGTQSVLGKiffsdffPYCGFLDDLSGLTAYMK------ECFERQDTYIQEVV 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 252 ETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDR 331
Cdd:PLN02966 253 NETLDPKRVKPETESMIDLLMEIYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVRE 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 332 VLGPGQLP--QPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQ 407
Cdd:PLN02966 333 YMKEKGSTfvTEDDVKNLPYFRALVKETLRIEPVIPlLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDE 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 408 FNPNHFLDAKGRFMKRG-AFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRpPAQT 486
Cdd:PLN02966 413 FRPERFLEKEVDFKGTDyEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPDDINMDVMTGLAMH-KSQH 491

                 ....*
gi 237681200 487 LCVVP 491
Cdd:PLN02966 492 LKLVP 496
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
64-485 1.22e-33

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 131.53  E-value: 1.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  64 ERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPiFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVqQ 143
Cdd:cd11043    3 KRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKS-VRKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEAL-K 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 144 PSMVGKVlQELACLkgQLDSYGGQP----LPLALLgwapcnITFTLLFGQRFDYQDPVFV-SLLSLIDQVMVLLGSPGIQ 218
Cdd:cd11043   81 DRLLGDI-DELVRQ--HLDSWWRGKsvvvLELAKK------MTFELICKLLLGIDPEEVVeELRKEFQAFLEGLLSFPLN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 219 LFNTfprlgaflRLHRPVLSKiEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDpeDMFGEANVLACTLDMVM 298
Cdd:cd11043  152 LPGT--------TFHRALKAR-KRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDG--DSLTDEEILDNILTLLF 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 299 AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVL---GPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADI 375
Cdd:cd11043  221 AGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAkrkEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDV 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFlDAKGRFMKRgAFLPFSAGRRVCVGKSLARTELFLLFAGLLQ 455
Cdd:cd11043  301 EYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW-EGKGKGVPY-TFLPFGGGPRLCPGAELAKLEILVFLHHLVT 378
                        410       420       430
                 ....*....|....*....|....*....|
gi 237681200 456 RYRLLPPPGLspaDLDLRPAPAFTMRPPAQ 485
Cdd:cd11043  379 RFRWEVVPDE---KISRFPLPRPPKGLPIR 405
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
28-442 1.39e-33

flavonoid 3',5'-hydroxylase (F3'5'H); Provisional


Pssm-ID: 177725  Cd Length: 504  Bit Score: 133.05  E-value: 1.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  28 PSLAPRWPPGPRPLPFLGNLHLLGVTQQdRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPI 107
Cdd:PLN00110  26 PKPSRKLPPGPRGWPLLGALPLLGNMPH-VALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 108 FQHIQRGGG--IFFSSGARWRAGRQFTvrTLQSLGVQ--------QPSMVGKVLQELACLkgqldSYGGQPLPLA-LLGW 176
Cdd:PLN00110 105 ATHLAYGAQdmVFADYGPRWKLLRKLS--NLHMLGGKaledwsqvRTVELGHMLRAMLEL-----SQRGEPVVVPeMLTF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 177 APCNITFTLLFGQR-FDYQDPVFVSLLSLIDQVMVLLGS-------PGIQLFNTFPRLGAFLRLHRP---VLSKIEEVRT 245
Cdd:PLN00110 178 SMANMIGQVILSRRvFETKGSESNEFKDMVVELMTTAGYfnigdfiPSIAWMDIQGIERGMKHLHKKfdkLLTRMIEEHT 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 246 IlrTLLETRRPPlptggpaqSYVEALLQQgQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRV 325
Cdd:PLN00110 258 A--SAHERKGNP--------DFLDVVMAN-QENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRA 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 326 QEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWET 404
Cdd:PLN00110 327 HEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPlNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWEN 406
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 237681200 405 PSQFNPNHFLDAK-GRFMKRG---AFLPFSAGRRVCVGKSLA 442
Cdd:PLN00110 407 PEEFRPERFLSEKnAKIDPRGndfELIPFGAGRRICAGTRMG 448
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
105-463 2.49e-33

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 130.84  E-value: 2.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 105 IPIFQHIQR-GGGIFFSSGARWRAGRQF--TVRTLQSLGVQQPSMVGKVLQELAclkgQLDSYGGQPLPLAllgwapCNI 181
Cdd:cd20621   38 FGPLGIDRLfGKGLLFSEGEEWKKQRKLlsNSFHFEKLKSRLPMINEITKEKIK----KLDNQNVNIIQFL------QKI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 182 T----FTLLFGQRF-DYQD-----PVFVSLLsLIDQVMVLLGSPGIQLFNT-FPRLGAFLRL---HRPVLSKIEEVRTIL 247
Cdd:cd20621  108 TgevvIRSFFGEEAkDLKIngkeiQVELVEI-LIESFLYRFSSPYFQLKRLiFGRKSWKLFPtkkEKKLQKRVKELRQFI 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 248 RTLLETR-----RPPLPTGGPAQSYVEALLQQGQEDDPEDmfgEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQ 322
Cdd:cd20621  187 EKIIQNRikqikKNKDEIKDIIIDLDLYLLQKKKLEQEIT---KEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQ 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 323 GRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHV-PRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQ 401
Cdd:cd20621  264 EKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLfPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKY 343
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237681200 402 WETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPP 463
Cdd:cd20621  344 FENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIP 405
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
64-462 2.64e-33

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 130.87  E-value: 2.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  64 ERYGPMFTIHLGSQKTVVLSGYEVVREALVGtGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQ-----FTVRTLQS 138
Cdd:cd11044   19 QKYGPVFKTHLLGRPTVFVIGAEAVRFILSG-EGKLVRYGWPRSVRRLLGENSLSLQDGEEHRRRRKllapaFSREALES 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 139 LgvqQPSMVGKVLQELA--CLKGQLDSYGgQPLPLALlgwapcNITFTLLFGQRFDYQDP-VFVSLLSLIDQVMVL-LGS 214
Cdd:cd11044   98 Y---VPTIQAIVQSYLRkwLKAGEVALYP-ELRRLTF------DVAARLLLGLDPEVEAEaLSQDFETWTDGLFSLpVPL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 215 PGIQLFntfprlgaflrlhRPVLSKiEEVRTILRTLLETRR--PPLPTGGPAQSYVEALLQQGQEDDPEDMFGEAnvlac 292
Cdd:cd11044  168 PFTPFG-------------RAIRAR-NKLLARLEQAIRERQeeENAEAKDALGLLLEAKDEDGEPLSMDELKDQA----- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 293 tLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPqPEHQRALPYTSAVLHEVQRyitLLPHVP---R 369
Cdd:cd11044  229 -LLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLT-LESLKKMPYLDQVIKEVLR---LVPPVGggfR 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 370 CTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL-----DAKGRFmkrgAFLPFSAGRRVCVGKSLART 444
Cdd:cd11044  304 KVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSparseDKKKPF----SLIPFGGGPRECLGKEFAQL 379
                        410       420
                 ....*....|....*....|
gi 237681200 445 ELFLLFAGLLQRYR--LLPP 462
Cdd:cd11044  380 EMKILASELLRNYDweLLPN 399
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
57-492 5.44e-33

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 130.00  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  57 RALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQrGGGIF--FSSGARW-RAGR---- 129
Cdd:cd11068    3 QSLLRLADELGPIFKLTLPGRRVVVVSSHDLIAELCDESRFDKKVSGPLEELRDFA-GDGLFtaYTHEPNWgKAHRilmp 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 130 QFTVRTLQSLgvqQPSMVgKVLQELaCLKgqLDSYGGqplplallgWAPCNIT--FTLL---------FGQRFD--YQD- 195
Cdd:cd11068   82 AFGPLAMRGY---FPMML-DIAEQL-VLK--WERLGP---------DEPIDVPddMTRLtldtialcgFGYRFNsfYRDe 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 196 -PVFV-SLLSLIDQVMVLLGSPGIQLFNTFPRlgaflrlHRPVLSKIEEVRTILRTLLETRRPpLPTGGPaqsyvEALLQ 273
Cdd:cd11068  146 pHPFVeAMVRALTEAGRRANRPPILNKLRRRA-------KRQFREDIALMRDLVDEIIAERRA-NPDGSP-----DDLLN 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 274 ---QGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPqPEHQRALPYT 350
Cdd:cd11068  213 lmlNGKDPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPP-YEQVAKLRYI 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 351 SAVLHEVQRyitLLPHVP---RCTAADIQLGG-YLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDakGRFMKR-- 423
Cdd:cd11068  292 RRVLDETLR---LWPTAPafaRKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLP--EEFRKLpp 366
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237681200 424 GAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPglspaDLDLRPAPAFTMRPPAQTLCVVPR 492
Cdd:cd11068  367 NAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP-----DYELDIKETLTLKPDGFRLKARPR 430
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
66-461 1.88e-32

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 128.47  E-value: 1.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQrGGGIFFSSGARWRagrqfTVRTLQSlgvqqPS 145
Cdd:cd11055    2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEPF-DSSLLFLKGERWK-----RLRTTLS-----PT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 146 --------MVGKV----------LQELACLKGQLDS---YGGqplplallgwapcnitFTL------LFGQRFDYQ---- 194
Cdd:cd11055   71 fssgklklMVPIIndccdelvekLEKAAETGKPVDMkdlFQG----------------FTLdvilstAFGIDVDSQnnpd 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 195 DPVFVS----LLSLIDQVMVLLGSPGIQLFntfprlGAFLRLHRPVLSKIEEVRTILRTLLETRRPPlpTGGPAQSYVEA 270
Cdd:cd11055  135 DPFLKAakkiFRNSIIRLFLLLLLFPLRLF------LFLLFPFVFGFKSFSFLEDVVKKIIEQRRKN--KSSRRKDLLQL 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 271 LL--QQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALP 348
Cdd:cd11055  207 MLdaQDSDEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLK 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 349 YTSAVLHEVQRyitLLPHVPRCT---AADIQLGGYLLPKGTPV-IPLLtSVLLDKTQWETPSQFNPNHFLDAKGRFMKRG 424
Cdd:cd11055  287 YLDMVINETLR---LYPPAFFISrecKEDCTINGVFIPKGVDVvIPVY-AIHHDPEFWPDPEKFDPERFSPENKAKRHPY 362
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 237681200 425 AFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP 461
Cdd:cd11055  363 AYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVP 399
PLN02655 PLN02655
ent-kaurene oxidase
36-438 5.09e-32

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 127.94  E-value: 5.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  36 PGprpLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGG 115
Cdd:PLN02655   5 PG---LPVIGNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 116 GIFFSS--GARWRAGRQFTVRTLqsLG--------VQQPSMVGKVLQELACLkgqLDSYGGQPL-----------PLAL- 173
Cdd:PLN02655  82 SMVATSdyGDFHKMVKRYVMNNL--LGanaqkrfrDTRDMLIENMLSGLHAL---VKDDPHSPVnfrdvfenelfGLSLi 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 174 --LGWAPCNItFTLLFGQRFDyQDPVFVSLLslidqVMVLLGSPGIQLFNTFPRLGAFL-RLHRPVLSKIEEVRT-ILRT 249
Cdd:PLN02655 157 qaLGEDVESV-YVEELGTEIS-KEEIFDVLV-----HDMMMCAIEVDWRDFFPYLSWIPnKSFETRVQTTEFRRTaVMKA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 250 LLETRRPPLPTGGPAQSYVEALLqqgqedDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEL 329
Cdd:PLN02655 230 LIKQQKKRIARGEERDCYLDFLL------SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREI 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 330 DRVLGpGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVP-RCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQF 408
Cdd:PLN02655 304 REVCG-DERVTEEDLPNLPYLNAVFHETLRKYSPVPLLPpRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEW 382
                        410       420       430
                 ....*....|....*....|....*....|
gi 237681200 409 NPNHFLDAKGRFMKRGAFLPFSAGRRVCVG 438
Cdd:PLN02655 383 DPERFLGEKYESADMYKTMAFGAGKRVCAG 412
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
300-482 5.36e-32

cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of vertebrate cytochrome P450 family 4, subfamily V (CYP4V) enzymes and similar proteins, including invertebrate subfamily C (CYP4C). Insect CYP4C enzymes may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. CYP4V2, the most characterized member of the CYP4V subfamily, is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 126.99  E-value: 5.36e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 300 GTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLP-QPEHQRALPYTSAVLHEVQRyitLLPHVP---RCTAADI 375
Cdd:cd20660  244 GHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDRPaTMDDLKEMKYLECVIKEALR---LFPSVPmfgRTLSEDI 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL--DAKGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGL 453
Cdd:cd20660  321 EIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLpeNSAGR--HPYAYIPFSAGPRNCIGQKFALMEEKVVLSSI 398
                        170       180
                 ....*....|....*....|....*....
gi 237681200 454 LQRYRLlppPGLSPADlDLRPAPAFTMRP 482
Cdd:cd20660  399 LRNFRI---ESVQKRE-DLKPAGELILRP 423
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
67-459 6.54e-32

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 126.95  E-value: 6.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALvgTGHELADRPPIPIFQHIQRGggIFFSSGARWRAGRQ-----FTVRTLQSLgv 141
Cdd:cd11057    1 GSPFRAWLGPRPFVITSDPEIVQVVL--NSPHCLNKSFFYDFFRLGRG--LFSAPYPIWKLQRKalnpsFNPKILLSF-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 142 qQPSMVGKVLQelacLKGQLDSYGGQPlPLALLgwaPCNITFTL------LFGQRFDYQDPVFVSLLSLIDQVMVLLG-- 213
Cdd:cd11057   75 -LPIFNEEAQK----LVQRLDTYVGGG-EFDIL---PDLSRCTLemicqtTLGSDVNDESDGNEEYLESYERLFELIAkr 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 214 --SPgiQLFNTF-PRLGAFLRLHRPVLSKIEE-VRTILRTLLETRRPPLPTGGP--------AQSYVEALLQ---QGQED 278
Cdd:cd11057  146 vlNP--WLHPEFiYRLTGDYKEEQKARKILRAfSEKIIEKKLQEVELESNLDSEedeengrkPQIFIDQLLElarNGEEF 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 279 DPEDMFGEANVlactldMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGP-GQLPQPEHQRALPYTSAVLHEV 357
Cdd:cd11057  224 TDEEIMDEIDT------MIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDdGQFITYEDLQQLVYLEMVLKET 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 358 QRYITLLPHVPRCTAADIQLG-GYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRV 435
Cdd:cd11057  298 MRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRN 377
                        410       420
                 ....*....|....*....|....
gi 237681200 436 CVGKSLARTELFLLFAGLLQRYRL 459
Cdd:cd11057  378 CIGWRYAMISMKIMLAKILRNYRL 401
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
66-484 2.88e-31

Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410692 [Multi-domain]  Cd Length: 437  Bit Score: 125.07  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIH-LGSQKTVVLSGYEVVREALVgtgHELADRPPIPIFQHIQR---GGGIFFSSGARWRAGRQ-----FTVRTL 136
Cdd:cd11069    1 YGGLIRYRgLFGSERLLVTDPKALKHILV---TNSYDFEKPPAFRRLLRrilGDGLLAAEGEEHKRQRKilnpaFSYRHV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 137 QSLgvqQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPcniTFTL------LFGQRFDY----QDPVFVSLLSLID 206
Cdd:cd11069   78 KEL---YPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLS---RATLdiiglaGFGYDFDSlenpDNELAEAYRRLFE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 207 QVMVLLGSPGIQLFNTFPRLGAF-LRLHRPVLSKIEEVRTILRTLLETRRpplptggpaqsyvEALLQQGQEDD------ 279
Cdd:cd11069  152 PTLLGSLLFILLLFLPRWLVRILpWKANREIRRAKDVLRRLAREIIREKK-------------AALLEGKDDSGkdilsi 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 280 --------PEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQR--ALPY 349
Cdd:cd11069  219 llrandfaDDERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDldRLPY 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 350 TSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKGR-----FMKR 423
Cdd:cd11069  299 LNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAaspggAGSN 378
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237681200 424 GAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGlspaDLDLRPAPAFTMRPPA 484
Cdd:cd11069  379 YALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPD----AEVERPIGIITRPPVD 435
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
67-492 9.50e-31

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 123.69  E-value: 9.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGG--IFFSSGARWRAGRQ------FTVRTLQS 138
Cdd:cd20657    1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQdmVFAPYGPRWRLLRKlcnlhlFGGKALED 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 139 LGVQQPSMVGKVLQELAclkgqLDSYGGQPLPLA-LLGWAPCNITFTLLFGQRfdyqdpVFVS--------LLSLIDQVM 209
Cdd:cd20657   81 WAHVRENEVGHMLKSMA-----EASRKGEPVVLGeMLNVCMANMLGRVMLSKR------VFAAkagakaneFKEMVVELM 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 210 VLLGspgiqLFNT---FPRL---------GAFLRLHRpvlskieEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQE 277
Cdd:cd20657  150 TVAG-----VFNIgdfIPSLawmdlqgveKKMKRLHK-------RFDALLTKILEEHKATAQERKGKPDFLDFVLLENDD 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 278 DDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEV 357
Cdd:cd20657  218 NGEGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKET 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 358 QRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLdaKGRFMK---RGA---FLPFS 430
Cdd:cd20657  298 FRLHPSTPlNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL--PGRNAKvdvRGNdfeLIPFG 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237681200 431 AGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRpPAQTLCVVPR 492
Cdd:cd20657  376 AGRRICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPEELNMEEAFGLALQ-KAVPLVAHPT 436
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
66-482 9.92e-31

Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP72 clan is associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 123.60  E-value: 9.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALvgTGHELA-DRPPIPIFQHIQRGGGIFFSSGARWRAGRQFT--VRTLQSLGVQ 142
Cdd:cd11052   11 YGKNFLYWYGTDPRLYVTEPELIKELL--SKKEGYfGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRIAnpAFHGEKLKGM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 143 QPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLID---QVMVLLGSPGIQL 219
Cdd:cd11052   89 VPAMVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLLRELQKicaQANRDVGIPGSRF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 220 FNTfPRLGAFLRLHRpvlskieEVRTILRTLLETRRPPLPTG--GPAQSYVEALLQQGQEDDPEDmfgeanvLACTLDMV 297
Cdd:cd11052  169 LPT-KGNKKIKKLDK-------EIEDSLLEIIKKREDSLKMGrgDDYGDDLLGLLLEANQSDDQN-------KNMTVQEI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 298 M--------AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQlPQPEHQRALPYTSAVLHEVQRYITLLPHVPR 369
Cdd:cd11052  234 VdecktfffAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDK-PPSDSLSKLKTVSMVINESLRLYPPAVFLTR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 370 CTAADIQLGGYLLPKGTPV-IPLLTsVLLDKTQW-ETPSQFNPNHFLD--AKGRFMKRgAFLPFSAGRRVCVGKSLARTE 445
Cdd:cd11052  313 KAKEDIKLGGLVIPKGTSIwIPVLA-LHHDEEIWgEDANEFNPERFADgvAKAAKHPM-AFLPFGLGPRNCIGQNFATME 390
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 237681200 446 LFLLFAGLLQRYRLlpppGLSPadlDLRPAPAF--TMRP 482
Cdd:cd11052  391 AKIVLAMILQRFSF----TLSP---TYRHAPTVvlTLRP 422
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
66-471 3.08e-30

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 122.42  E-value: 3.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  66 YGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIF------FSSGARWR---AGRQFTVRTL 136
Cdd:cd11066    1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTFHKVVSSTQGFtigtspWDESCKRRrkaAASALNRPAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 137 QS----LGVQQPSMVGKVLQELACLKGQLDsyggqPLP----LALlgwapcNITFTLLFGQRFD--YQDPVFVSLLSLID 206
Cdd:cd11066   81 QSyapiIDLESKSFIRELLRDSAEGKGDID-----PLIyfqrFSL------NLSLTLNYGIRLDcvDDDSLLLEIIEVES 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 207 QVMvLLGSPGIQLFNTFPrlgaFLRLHRPVLSKIEEVRTILR-------TLLETRRPPLPTGGPAQSYVEALLQqgqedD 279
Cdd:cd11066  150 AIS-KFRSTSSNLQDYIP----ILRYFPKMSKFRERADEYRNrrdkylkKLLAKLKEEIEDGTDKPCIVGNILK-----D 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 280 PEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPH--VQGRVQEELDRVlGPGQLPQPEH---QRALPYTSAVL 354
Cdd:cd11066  220 KESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGqeIQEKAYEEILEA-YGNDEDAWEDcaaEEKCPYVVALV 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 355 HEVQRYITLLP-HVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGR 433
Cdd:cd11066  299 KETLRYFTVLPlGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGS 378
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 237681200 434 RVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLD 471
Cdd:cd11066  379 RMCAGSHLANRELYTAICRLILLFRIGPKDEEEPMELD 416
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
67-455 5.00e-30

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 121.55  E-value: 5.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALvgTGHEL--ADRPPIPIFQHIQRGGGIFFSS--GARWRAGRQFTV------RTL 136
Cdd:cd20655    1 GPLLHLRIGSVPCVVVSSASVAKEIL--KTHDLnfSSRPVPAAAESLLYGSSGFAFApyGDYWKFMKKLCMtellgpRAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 137 -QSLGV--QQPSMVGKVLQELACLKGQLDsYGGQPLPLAllgwapCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLG 213
Cdd:cd20655   79 eRFRPIraQELERFLRRLLDKAEKGESVD-IGKELMKLT------NNIICRMIMGRSCSEENGEAEEVRKLVKESAELAG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 214 SpgiqlFNtfprLGAFLRLHRPV-LS----KIEEVRTILRTLLET------RRPPLPTGGPAQSYVEALLQQGQEDDPED 282
Cdd:cd20655  152 K-----FN----ASDFIWPLKKLdLQgfgkRIMDVSNRFDELLERiikeheEKRKKRKEGGSKDLLDILLDAYEDENAEY 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 283 MFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYIT 362
Cdd:cd20655  223 KITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHP 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 363 LLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL---------DAKGRFMKrgaFLPFSAGR 433
Cdd:cd20655  303 PGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLassrsgqelDVRGQHFK---LLPFGSGR 379
                        410       420
                 ....*....|....*....|..
gi 237681200 434 RVCVGKSLARTELFLLFAGLLQ 455
Cdd:cd20655  380 RGCPGASLAYQVVGTAIAAMVQ 401
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
67-455 3.27e-29

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 119.25  E-value: 3.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  67 GPMFTIHLGSQKTVVLSGYEVVREALvgTGHE--LADRPPIPIFQHIQRGGGIFFSS--GARWRAGRQFTvrTLQ----- 137
Cdd:cd20653    1 GPIFSLRFGSRLVVVVSSPSAAEECF--TKNDivLANRPRFLTGKHIGYNYTTVGSApyGDHWRNLRRIT--TLEifssh 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 138 SLGVQQPSMVGKVLQELACLkgqLDSYGGQPLPLALLGWAPC---NITFTLLFGQRFDYQDPVFV----SLLSLIDQVMV 210
Cdd:cd20653   77 RLNSFSSIRRDEIRRLLKRL---ARDSKGGFAKVELKPLFSEltfNNIMRMVAGKRYYGEDVSDAeeakLFRELVSEIFE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 211 LLGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGpaQSYVEALLQQgQEDDPEdMFGEANVL 290
Cdd:cd20653  154 LSGAGNPADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGK--NTMIDHLLSL-QESQPE-YYTDEIIK 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 291 ACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPH-VPR 369
Cdd:cd20653  230 GLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLlVPH 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 370 CTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFldaKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLL 449
Cdd:cd20653  310 ESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF---EGEEREGYKLIPFGLGRRACPGAGLAQRVVGLA 386

                 ....*.
gi 237681200 450 FAGLLQ 455
Cdd:cd20653  387 LGSLIQ 392
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
295-467 8.78e-29

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 118.10  E-value: 8.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAAD 374
Cdd:cd20647  244 EMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGRVTQDD 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 375 IQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL--DAKGRFMKRGAfLPFSAGRRVCVGKSLARTELFLLFAG 452
Cdd:cd20647  324 LIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLrkDALDRVDNFGS-IPFGYGIRSCIGRRIAELEIHLALIQ 402
                        170
                 ....*....|....*
gi 237681200 453 LLQRYRLLPPPGLSP 467
Cdd:cd20647  403 LLQNFEIKVSPQTTE 417
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
296-464 9.93e-29

cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 117.85  E-value: 9.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 296 MVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRyitLLPHVP----RCT 371
Cdd:cd11046  248 MLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLR---LYPQPPvlirRAV 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 372 AADIqlggylLPKGTPVIPLLTSVLL-------DKTQWETPSQFNPNHFLDAKGRFMKRG----AFLPFSAGRRVCVGKS 440
Cdd:cd11046  325 EDDK------LPGGGVKVPAGTDIFIsvynlhrSPELWEDPEEFDPERFLDPFINPPNEViddfAFLPFGGGPRKCLGDQ 398
                        170       180
                 ....*....|....*....|....
gi 237681200 441 LARTELFLLFAGLLQRYRLLPPPG 464
Cdd:cd11046  399 FALLEATVALAMLLRRFDFELDVG 422
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
117-474 5.51e-28

cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 115.71  E-value: 5.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 117 IFFSSGARWRAGRQ-----FT---VRTLQSLGVQqpsmVGKVLQElaclkgQLDSYGGQPLPLALLGWAPC---NITFTL 185
Cdd:cd11056   53 LFSLDGEKWKELRQkltpaFTsgkLKNMFPLMVE----VGDELVD------YLKKQAEKGKELEIKDLMARyttDVIASC 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 186 LFG---QRFDYQDPVFVSL------LSLIDQVMVLLgspgiqlFNTFPRLGAFLRLhRPVLSKIEE-VRTILRTLLETRR 255
Cdd:cd11056  123 AFGldaNSLNDPENEFREMgrrlfePSRLRGLKFML-------LFFFPKLARLLRL-KFFPKEVEDfFRKLVRDTIEYRE 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 256 PplpTGGPAQSYVEALLQQGQEDDPEDMFGEANVlacTLDMV--------MAGTETTAATLQWAVFLMVKHPHVQGRVQE 327
Cdd:cd11056  195 K---NNIVRNDFIDLLLELKKKGKIEDDKSEKEL---TDEELaaqafvffLAGFETSSSTLSFALYELAKNPEIQEKLRE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 328 ELDRVL--GPGQLpQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGG--YLLPKGTPV-IPLLtSVLLDKTQW 402
Cdd:cd11056  269 EIDEVLekHGGEL-TYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPViIPVY-ALHHDPKYY 346
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237681200 403 ETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP------PPGLSPADLDLRP 474
Cdd:cd11056  347 PEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPssktkiPLKLSPKSFVLSP 424
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
185-457 8.00e-28

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 114.99  E-value: 8.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 185 LLFGQRFDY------QDPVFVSLLSLIDQVMVLLGSPGIQ-LFNTFPrlgafLRLHRPVLSKIEEVRTILRTLLETRRPP 257
Cdd:cd11060  118 ITFGKPFGFleagtdVDGYIASIDKLLPYFAVVGQIPWLDrLLLKNP-----LGPKRKDKTGFGPLMRFALEAVAERLAE 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 258 LPTGGPA-----QSYVEALLQQGQEDDPEDMFGEANVlactldMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRV 332
Cdd:cd11060  193 DAESAKGrkdmlDSFLEAGLKDPEKVTDREVVAEALS------NILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 333 LGPGQLPQP---EHQRALPYTSAVLHEVQRY----ITLLP-HVPRCtaaDIQLGGYLLPKGTpVIPLLTSVLL-DKTQW- 402
Cdd:cd11060  267 VAEGKLSSPitfAEAQKLPYLQAVIKEALRLhppvGLPLErVVPPG---GATICGRFIPGGT-IVGVNPWVIHrDKEVFg 342
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 237681200 403 ETPSQFNPNHFLDAKG--RFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRY 457
Cdd:cd11060  343 EDADVFRPERWLEADEeqRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRF 399
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
186-457 9.23e-28

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 115.04  E-value: 9.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 186 LFGQRFDY-QDPVFVSLLSLidqvMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKI------------EEVRTILRTLLE 252
Cdd:cd11062  117 AFGRSYGYlDEPDFGPEFLD----ALRALAEMIHLLRHFPWLLKLLRSLPESLLKRlnpglavfldfqESIAKQVDEVLR 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 253 TRRPPLPTGGPAQSYVEALLQQ--GQEDDPEDMFGEAnvlactLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELD 330
Cdd:cd11062  193 QVSAGDPPSIVTSLFHALLNSDlpPSEKTLERLADEA------QTLIGAGTETTARTLSVATFHLLSNPEILERLREELK 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 331 RVL-GPGQLPQPEHQRALPYTSAVLHEVQRYITLLPH-VPR-CTAADIQLGGYLLPKGTPV---IPLltsVLLDKTQWET 404
Cdd:cd11062  267 TAMpDPDSPPSLAELEKLPYLTAVIKEGLRLSYGVPTrLPRvVPDEGLYYKGWVIPPGTPVsmsSYF---VHHDEEIFPD 343
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 237681200 405 PSQFNPNHFLDAKGRF-MKRgaFL-PFSAGRRVCVGKSLARTELFLLFAGLLQRY 457
Cdd:cd11062  344 PHEFRPERWLGAAEKGkLDR--YLvPFSKGSRSCLGINLAYAELYLALAALFRRF 396
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
185-464 1.38e-27

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 114.24  E-value: 1.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 185 LLFGQRFDY-QDPVFVSLLSLIDQVMVLLG--SPGIQLFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPtg 261
Cdd:cd11061  117 LAFGKSFGMlESGKDRYILDLLEKSMVRLGvlGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQLKERLKAEEEKRP-- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 262 gpaqSYVEALLQ-----QGQEDDPEDMFGEANVLactldmVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVL-GP 335
Cdd:cd11061  195 ----DIFSYLLEakdpeTGEGLDLEELVGEARLL------IVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFpSD 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 336 GQLPQPEHQRALPYTSAVLHEVQRyitLLPHVP----RCTAAD-IQLGGYLLPKGTPV-IPLLTsvlL--DKTQWETPSQ 407
Cdd:cd11061  265 DEIRLGPKLKSLPYLRACIDEALR---LSPPVPsglpRETPPGgLTIDGEYIPGGTTVsVPIYS---IhrDERYFPDPFE 338
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 237681200 408 FNPNHFLDAKGRFMK-RGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPG 464
Cdd:cd11061  339 FIPERWLSRPEELVRaRSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPG 396
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
299-475 2.40e-26

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 111.07  E-value: 2.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 299 AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRyitLLPHVP---RCTAADI 375
Cdd:cd20613  245 AGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLR---LYPPVPgtsRELTKDI 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIpLLTSVL--LDKTqWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGL 453
Cdd:cd20613  322 ELGGYKIPAGTTVL-VSTYVMgrMEEY-FEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKL 399
                        170       180
                 ....*....|....*....|....*
gi 237681200 454 LQRYRLLPPPGLSPADLD---LRPA 475
Cdd:cd20613  400 LQNFKFELVPGQSFGILEevtLRPK 424
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
291-459 4.18e-26

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 110.28  E-value: 4.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 291 ACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRC 370
Cdd:cd20645  229 AAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRT 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 371 TAADIQLGGYLLPKGTpVIPLLTSVL-LDKTQWETPSQFNPNHFLDAKgRFMKRGAFLPFSAGRRVCVGKSLARTELFLL 449
Cdd:cd20645  309 LDKDTVLGDYLLPKGT-VLMINSQALgSSEEYFEDGRQFKPERWLQEK-HSINPFAHVPFGIGKRMCIGRRLAELQLQLA 386
                        170
                 ....*....|
gi 237681200 450 FAGLLQRYRL 459
Cdd:cd20645  387 LCWIIQKYQI 396
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
63-482 6.37e-26

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 109.85  E-value: 6.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  63 SERYGPMFTIHLGSQKTVVLSGYEVVREALV-GTGHElaDR----PPIPIFQhiqrGGGIFFSSGARWRAGRQ-----FT 132
Cdd:cd20639    8 RKIYGKTFLYWFGPTPRLTVADPELIREILLtRADHF--DRyeahPLVRQLE----GDGLVSLRGEKWAHHRRvitpaFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 133 VRTLQSLgvqQPSMVGKVLQELACLKGQLDSYGGQPLPLAllGWApCN-----ITFTLlFGQRFDYQDPVFvsllSLIDQ 207
Cdd:cd20639   82 MENLKRL---VPHVVKSVADMLDKWEAMAEAGGEGEVDVA--EWF-QNltedvISRTA-FGSSYEDGKAVF----RLQAQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 208 VMVLLGS-------PGIQLFNTfprlgaflRLHRPVLSKIEEVRTILRTLLETRR---PPLPTGGPAQSYVEALLQQGQE 277
Cdd:cd20639  151 QMLLAAEafrkvyiPGYRFLPT--------KKNRKSWRLDKEIRKSLLKLIERRQtaaDDEKDDEDSKDLLGLMISAKNA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 278 DDPEDMFGEANVLACTlDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEV 357
Cdd:cd20639  223 RNGEKMTVEEIIEECK-TFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNET 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 358 QRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKGRFMKR-GAFLPFSAGRRV 435
Cdd:cd20639  302 LRLYPPAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHpLAFIPFGLGPRT 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 237681200 436 CVGKSLARTELFLLFAGLLQRYRLLPPPGLSPAdldlrPAPAFTMRP 482
Cdd:cd20639  382 CVGQNLAILEAKLTLAVILQRFEFRLSPSYAHA-----PTVLMLLQP 423
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
63-468 1.55e-25

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 108.65  E-value: 1.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  63 SERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELAdrPPI-------PIFqhiqrGGGIFFSSGARWRAGR-----Q 130
Cdd:cd20640    8 RKQYGPIFTYSTGNKQFLYVSRPEMVKEINLCVSLDLG--KPSylkktlkPLF-----GGGILTSNGPHWAHQRkiiapE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 131 FTVRTLQSLgVQQpsMVGKVLQELACLKGQLDSYGGQPLPLAL---LGWAPCNITFTLLFGQRFDYQDPVFV---SLLSL 204
Cdd:cd20640   81 FFLDKVKGM-VDL--MVDSAQPLLSSWEERIDRAGGMAADIVVdedLRAFSADVISRACFGSSYSKGKEIFSklrELQKA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 205 IDQVMVLLGSPGIQLFNTFPRLGAFlRLHRpvlskieEVRT-ILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDM 283
Cdd:cd20640  158 VSKQSVLFSIPGLRHLPTKSNRKIW-ELEG-------EIRSlILEIVKEREEECDHEKDLLQAILEGARSSCDKKAEAED 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 284 FGEANvlaCTlDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRYITL 363
Cdd:cd20640  230 FIVDN---CK-NIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRMKTVTMVIQETLRLYPP 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 364 LPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKGRFMKR-GAFLPFSAGRRVCVGKSL 441
Cdd:cd20640  305 AAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPpHSYMPFGAGARTCLGQNF 384
                        410       420
                 ....*....|....*....|....*....
gi 237681200 442 ARTELFLLFAGLLQRYRLLPPPGL--SPA 468
Cdd:cd20640  385 AMAELKVLVSLILSKFSFTLSPEYqhSPA 413
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
294-489 1.50e-23

unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized fungal cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 102.76  E-value: 1.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRV-LGPGQLPQPEHQRALPYTSAVLHEVQRyitLLPHV----P 368
Cdd:cd11059  227 LDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLpGPFRGPPDLEDLDKLPYLNAVIRETLR---LYPPIpgslP 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 369 RCTAAD-IQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKG---RFMKRgAFLPFSAGRRVCVGKSLART 444
Cdd:cd11059  304 RVVPEGgATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGetaREMKR-AFWPFGSGSRMCIGMNLALM 382
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 237681200 445 ELFLLFAGLLQRYRllpppGLSPADLDLRPAPAFTMRPPAQTLCV 489
Cdd:cd11059  383 EMKLALAAIYRNYR-----TSTTTDDDMEQEDAFLAAPKGRRCLL 422
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
106-464 2.45e-23

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 102.28  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 106 PIFQHIQR---GGGIFFSSGARWRAGRQ-----FTVRTLQSLgvqqpsMVGKVLQELACLKGQLDSY---GGQPLPL-AL 173
Cdd:cd11064   37 PEFRDLFFdllGDGIFNVDGELWKFQRKtasheFSSRALREF------MESVVREKVEKLLVPLLDHaaeSGKVVDLqDV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 174 LGWAPCNITFTLLFGQrfdyqDPVFVSllslidqvMVLLGSPGIQLFNTFPRLgAFLRLHRPV-LSKI------------ 240
Cdd:cd11064  111 LQRFTFDVICKIAFGV-----DPGSLS--------PSLPEVPFAKAFDDASEA-VAKRFIVPPwLWKLkrwlnigsekkl 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 241 -EEVRTI-------LRTLLETRRPPLPTGGPAQ----SYVEALLQQGQEDDPEDMFgeanvlactlDMVM----AGTETT 304
Cdd:cd11064  177 rEAIRVIddfvyevISRRREELNSREEENNVREdllsRFLASEEEEGEPVSDKFLR----------DIVLnfilAGRDTT 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 305 AATLQWAVFLMVKHPHVQGRVQEELDRVL-----GPGQLPQPEHQRALPYTSAVLHEVQRyitLLPHVP----RCTAADI 375
Cdd:cd11064  247 AAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLR---LYPPVPfdskEAVNDDV 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKGRFMKRGA--FLPFSAGRRVCVGKSLARTELFLLFAG 452
Cdd:cd11064  324 LPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLRPESPykFPAFNAGPRICLGKDLAYLQMKIVAAA 403
                        410
                 ....*....|..
gi 237681200 453 LLQRYRLLPPPG 464
Cdd:cd11064  404 ILRRFDFKVVPG 415
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
296-469 4.05e-23

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 101.14  E-value: 4.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 296 MVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLG-PGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAAD 374
Cdd:cd11042  220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGdGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKP 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 375 IQL--GGYLLPKGTPVI--PLLTSVllDKTQWETPSQFNPNHFLDAKGRFMKRG--AFLPFSAGRRVCVGKSLARTELFL 448
Cdd:cd11042  300 FEVegGGYVIPKGHIVLasPAVSHR--DPEIFKNPDEFDPERFLKGRAEDSKGGkfAYLPFGAGRHRCIGENFAYLQIKT 377
                        170       180
                 ....*....|....*....|..
gi 237681200 449 LFAGLLQRYRL-LPPPGLSPAD 469
Cdd:cd11042  378 ILSTLLRNFDFeLVDSPFPEPD 399
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
33-461 7.16e-23

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 101.21  E-value: 7.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  33 RWPPGPRPLPFLG-NLHLLGVTQQDRA---LMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIF 108
Cdd:PLN02987  30 RLPPGSLGLPLVGeTLQLISAYKTENPepfIDERVARYGSLFMTHLFGEPTVFSADPETNRFILQNEGKLFECSYPGSIS 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 109 QHIQRGGgIFFSSGARWRAGRQFTVRTLQSLGVQQPSMVGkvLQELacLKGQLDSYGGQplplALLGWAPCNITFTLLFG 188
Cdd:PLN02987 110 NLLGKHS-LLLMKGNLHKKMHSLTMSFANSSIIKDHLLLD--IDRL--IRFNLDSWSSR----VLLMEEAKKITFELTVK 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 189 QRFDYqDPVFVSLLSLIDQVMVLLGspgiqlFNTFPrLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQS-Y 267
Cdd:PLN02987 181 QLMSF-DPGEWTESLRKEYVLVIEG------FFSVP-LPLFSTTYRRAIQARTKVAEALTLVVMKRRKEEEEGAEKKKdM 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 268 VEALLqqgqedDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLG----PGQLPQPEH 343
Cdd:PLN02987 253 LAALL------ASDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAmksdSYSLEWSDY 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 344 qRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKR 423
Cdd:PLN02987 327 -KSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPS 405
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 237681200 424 GAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP 461
Cdd:PLN02987 406 NVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVP 443
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
258-463 2.69e-22

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 98.96  E-value: 2.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 258 LPTGGPAQS-YVEALLQQGQeddpedmFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPG 336
Cdd:cd20646  209 VDRGEPVEGeYLTYLLSSGK-------LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGD 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 337 QLPQPEHQRALPYTSAVLHEVQRyitLLPHVP---RCTA-ADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNH 412
Cdd:cd20646  282 RIPTAEDIAKMPLLKAVIKETLR---LYPVVPgnaRVIVeKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPER 358
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 237681200 413 FLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPP 463
Cdd:cd20646  359 WLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVRPDP 409
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
92-457 3.51e-22

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 98.48  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  92 LVGTGHELAD---------RPPI--PIFQHIQRGGGIFFSSGARWRAGRQ-----FTVRTLQSLgvqQPSMVGKVLQELA 155
Cdd:cd11051   13 LVVTDPELAEqitqvtnlpKPPPlrKFLTPLTGGSSLISMEGEEWKRLRKrfnpgFSPQHLMTL---VPTILDEVEIFAA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 156 CLKGQLDSygGQPLPLALLGwapCNITFTLL----FGQRFDYQ-DPVFVSLLslidqvMVLLGSPGIQLFNTFPRLGAFL 230
Cdd:cd11051   90 ILRELAES--GEVFSLEELT---TNLTFDVIgrvtLDIDLHAQtGDNSLLTA------LRLLLALYRSLLNPFKRLNPLR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 231 RLHRPVLSKIeeVRTILRTLLETRrpplptggpaqsyveallqqgqeddpedmFGEANVLACTLDMVMAGTETTAATLQW 310
Cdd:cd11051  159 PLRRWRNGRR--LDRYLKPEVRKR-----------------------------FELERAIDQIKTFLFAGHDTTSSTLCW 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 311 AVFLMVKHPHVQGRVQEELDRVLGPG------QLPQPEHQ-RALPYTSAVLHEVQRyitLLP--HVPRCTAADIQL---- 377
Cdd:cd11051  208 AFYLLSKHPEVLAKVRAEHDEVFGPDpsaaaeLLREGPELlNQLPYTTAVIKETLR---LFPpaGTARRGPPGVGLtdrd 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 378 GGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMK--RGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQ 455
Cdd:cd11051  285 GKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYppKSAWRPFERGPRNCIGQELAMLELKIILAMTVR 364

                 ..
gi 237681200 456 RY 457
Cdd:cd11051  365 RF 366
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
295-467 5.67e-22

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 97.90  E-value: 5.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTA-A 373
Cdd:cd20648  241 ELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPdR 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 374 DIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDaKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGL 453
Cdd:cd20648  321 DIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLG-KGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARI 399
                        170
                 ....*....|....
gi 237681200 454 LQRYRLLPPPGLSP 467
Cdd:cd20648  400 LTHFEVRPEPGGSP 413
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
195-466 1.21e-21

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 97.76  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 195 DPVFVSLLSLIDQVMVLLGSPgiqlfntFPRLGAFLRLHRPVLSKIEEVRT-ILRTLLETRRPPLP---TGGPAQSYVEA 270
Cdd:cd20622  168 PDELEAVLDLADSVEKSIKSP-------FPKLSHWFYRNQPSYRRAAKIKDdFLQREIQAIARSLErkgDEGEVRSAVDH 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 271 LLQQ----GQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGP----GQLPQPE 342
Cdd:cd20622  241 MVRRelaaAEKEGRKPDYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEavaeGRLPTAQ 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 343 HQRA--LPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIpLLT---SVLLD------------------K 399
Cdd:cd20622  321 EIAQarIPYLDAVIEEILRCANTAPILSREATVDTQVLGYSIPKGTNVF-LLNngpSYLSPpieidesrrssssaakgkK 399
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237681200 400 TQW---ETPSQFNPNHFLDAKGRFM------KRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP-PPGLS 466
Cdd:cd20622  400 AGVwdsKDIADFDPERWLVTDEETGetvfdpSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPlPEALS 476
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
299-482 1.70e-21

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 96.75  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 299 AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLG 378
Cdd:cd20641  246 AGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLG 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 379 GYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKGRFMKR-GAFLPFSAGRRVCVGKSLARTELFLLFAGLLQR 456
Cdd:cd20641  326 GLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHpNALLSFSLGPRACIGQNFAMIEAKTVLAMILQR 405
                        170       180
                 ....*....|....*....|....*.
gi 237681200 457 YRLlpppGLSPaDLDLRPAPAFTMRP 482
Cdd:cd20641  406 FSF----SLSP-EYVHAPADHLTLQP 426
PLN02302 PLN02302
ent-kaurenoic acid oxidase
294-461 2.12e-21

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 96.71  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVM-AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLgpgqLPQPEHQ--------RALPYTSAVLHEVQRYITLL 364
Cdd:PLN02302 292 LLMYLnAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIA----KKRPPGQkgltlkdvRKMEYLSQVIDETLRLINIS 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 365 PHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKgrfMKRGAFLPFSAGRRVCVGKSLART 444
Cdd:PLN02302 368 LTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYT---PKAGTFLPFGLGSRLCPGNDLAKL 444
                        170
                 ....*....|....*..
gi 237681200 445 ELFLLFAGLLQRYRLLP 461
Cdd:PLN02302 445 EISIFLHHFLLGYRLER 461
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
300-457 2.36e-21

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 96.37  E-value: 2.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 300 GTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQP-EHQRALPYTSAVLHEVQRyitLLPHVP---RCTAADI 375
Cdd:cd20680  255 GHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPVTmEDLKKLRYLECVIKESLR---LFPSVPlfaRSLCEDC 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL--DAKGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGL 453
Cdd:cd20680  332 EIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFpeNSSGR--HPYAYIPFSAGPRNCIGQRFALMEEKVVLSCI 409

                 ....
gi 237681200 454 LQRY 457
Cdd:cd20680  410 LRHF 413
PLN02936 PLN02936
epsilon-ring hydroxylase
294-464 3.30e-21

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 96.40  E-value: 3.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRyitLLPHVP----R 369
Cdd:PLN02936 284 LSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMR---LYPHPPvlirR 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 370 CTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGA---FLPFSAGRRVCVGKSLARTEL 446
Cdd:PLN02936 360 AQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTdfrYIPFSGGPRKCVGDQFALLEA 439
                        170
                 ....*....|....*...
gi 237681200 447 FLLFAGLLQRYRLLPPPG 464
Cdd:PLN02936 440 IVALAVLLQRLDLELVPD 457
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
225-457 3.50e-21

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 95.70  E-value: 3.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 225 RLGAFLRLHRPVLSK--IEEVRT-----ILRTLLETRRPPLPTGGPAQSYVEALLQQGQedDPEDMFGEA-NVLactldm 296
Cdd:cd11063  154 RLGKLLWLLRDKKFReaCKVVHRfvdpyVDKALARKEESKDEESSDRYVFLDELAKETR--DPKELRDQLlNIL------ 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 297 vMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRyitLLPHVP---RCTAA 373
Cdd:cd11063  226 -LAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLR---LYPPVPlnsRVAVR 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 374 DIQL---GG------YLLPKGTPViplLTSVLL---DKTQW-ETPSQFNPNHFLDAKgrfmKRG-AFLPFSAGRRVCVGK 439
Cdd:cd11063  302 DTTLprgGGpdgkspIFVPKGTRV---LYSVYAmhrRKDIWgPDAEEFRPERWEDLK----RPGwEYLPFNGGPRICLGQ 374
                        250
                 ....*....|....*...
gi 237681200 440 SLARTELFLLFAGLLQRY 457
Cdd:cd11063  375 QFALTEASYVLVRLLQTF 392
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
277-477 7.34e-21

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 94.31  E-value: 7.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 277 EDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRvLGPGQLPQpEHQRALPYTSAVLHE 356
Cdd:cd11045  200 EDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLA-LGKGTLDY-EDLGQLEVTDWVFKE 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 357 VQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFL-----DAKGRFmkrgAFLPFSA 431
Cdd:cd11045  278 ALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSperaeDKVHRY----AWAPFGG 353
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 237681200 432 GRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLR-PAPA 477
Cdd:cd11045  354 GAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPPWWQSPlPAPK 400
PLN02738 PLN02738
carotene beta-ring hydroxylase
296-470 1.05e-20

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 95.36  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 296 MVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGqLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADI 375
Cdd:PLN02738 399 MLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDR-FPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLEND 477
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHF-LDAKG--RFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAG 452
Cdd:PLN02738 478 MLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpLDGPNpnETNQNFSYLPFGGGPRKCVGDMFASFENVVATAM 557
                        170
                 ....*....|....*...
gi 237681200 453 LLQRYRLLPPPGLSPADL 470
Cdd:PLN02738 558 LVRRFDFQLAPGAPPVKM 575
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
291-492 1.28e-20

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 93.97  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 291 ACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAV------LHEVQRYItlL 364
Cdd:cd20658  240 AQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACareafrLHPVAPFN--V 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 365 PHVPRctaADIQLGGYLLPKGTPVipLLTSVLLDKTQ--WETPSQFNPNhfldakgRFMKRGA----------FLPFSAG 432
Cdd:cd20658  318 PHVAM---SDTTVGGYFIPKGSHV--LLSRYGLGRNPkvWDDPLKFKPE-------RHLNEDSevtltepdlrFISFSTG 385
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 433 RRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRPpaQTLCVVPR 492
Cdd:cd20658  386 RRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSVDLSESKDDLFMAKP--LVLVAKPR 443
PLN02290 PLN02290
cytokinin trans-hydroxylase
234-482 1.79e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 94.11  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 234 RPVLSKIEEVRTILRTLLETRRPPLPTGgPAQSY---VEALLQQGQEDDPEDMFGeanvlaCTLDMVM--------AGTE 302
Cdd:PLN02290 258 REIKSLKGEVERLLMEIIQSRRDCVEIG-RSSSYgddLLGMLLNEMEKKRSNGFN------LNLQLIMdecktfffAGHE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 303 TTAATLQWAVFLMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRYI---TLLphvPRCTAADIQLGG 379
Cdd:PLN02290 331 TTALLLTWTLMLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYppaTLL---PRMAFEDIKLGD 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 380 YLLPKGTPV-IPLLtSVLLDKTQW-ETPSQFNPNHFldAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRY 457
Cdd:PLN02290 407 LHIPKGLSIwIPVL-AIHHSEELWgKDANEFNPDRF--AGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKF 483
                        250       260
                 ....*....|....*....|....*..
gi 237681200 458 RLlpppGLSPadlDLRPAP--AFTMRP 482
Cdd:PLN02290 484 SF----TISD---NYRHAPvvVLTIKP 503
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
261-486 4.41e-20

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 92.12  E-value: 4.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 261 GGPAQSYVEALLQQgqEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVlgpGQLP- 339
Cdd:cd20614  183 NGARTGLVAALIRA--RDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA---GDVPr 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 340 QPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKgR 419
Cdd:cd20614  258 TPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRD-R 336
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 237681200 420 FMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLqryRLLPPPGLSPADLDLRPAPAF--TMRPPAQT 486
Cdd:cd20614  337 APNPVELLQFGGGPHFCLGYHVACVELVQFIVALA---RELGAAGIRPLLVGVLPGRRYfpTLHPSNKT 402
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
185-454 6.50e-20

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 91.87  E-value: 6.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 185 LLFGQRFD------YQDPVFVSLLSLIDQVMvllgspgIQLFNTFPRLGAFLRL--HRPVLSKIEEVRTILRTLLETRrp 256
Cdd:cd11058  119 LAFGESFGclengeYHPWVALIFDSIKALTI-------IQALRRYPWLLRLLRLliPKSLRKKRKEHFQYTREKVDRR-- 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 257 pLPTGGPAQSYVEALLQQGQEDD---PEDMFGEANVLactldmVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELdRvl 333
Cdd:cd11058  190 -LAKGTDRPDFMSYILRNKDEKKgltREELEANASLL------IIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-R-- 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 334 gpGQLPQPEH-----QRALPYTSAVLHEVQRyitLLPHVP-----RCTAADIQLGGYLLPKGTPV-IPLLTSVLlDKTQW 402
Cdd:cd11058  260 --SAFSSEDDitldsLAQLPYLNAVIQEALR---LYPPVPaglprVVPAGGATIDGQFVPGGTSVsVSQWAAYR-SPRNF 333
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 237681200 403 ETPSQFNPNHFL-DAKGRFM--KRGAFLPFSAGRRVCVGKSLARTELFLLFAGLL 454
Cdd:cd11058  334 HDPDEFIPERWLgDPRFEFDndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLL 388
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
242-482 8.14e-20

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 91.57  E-value: 8.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 242 EVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLacTLDMVM--------AGTETTAATLQWAVF 313
Cdd:cd20642  182 EIRSSLRGIINKREKAMKAGEATNDDLLGILLESNHKEIKEQGNKNGGM--STEDVIeecklfyfAGQETTSVLLVWTMV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 314 LMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPV-IPLL 392
Cdd:cd20642  260 LLSQHPDWQERAREEVLQVFG-NNKPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVsLPIL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 393 tsvLL--DKTQW-ETPSQFNPNHFLD-----AKGRFMkrgaFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLlpppG 464
Cdd:cd20642  339 ---LVhrDPELWgDDAKEFNPERFAEgiskaTKGQVS----YFPFGWGPRICIGQNFALLEAKMALALILQRFSF----E 407
                        250
                 ....*....|....*...
gi 237681200 465 LSPADLDLrPAPAFTMRP 482
Cdd:cd20642  408 LSPSYVHA-PYTVLTLQP 424
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
35-459 3.74e-19

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 89.99  E-value: 3.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  35 PPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELadRPPIPIFQHIQRG 114
Cdd:PLN02196  37 PPGTMGWPYVGETFQLYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLF--KPTFPASKERMLG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 115 G-GIFFSSGARWRAGRQFTVRTLQSLGVQqpSMVGKVlQELAclKGQLDSYGGQPLPlallgwapcniTFTLLFGQRFDy 193
Cdd:PLN02196 115 KqAIFFHQGDYHAKLRKLVLRAFMPDAIR--NMVPDI-ESIA--QESLNSWEGTQIN-----------TYQEMKTYTFN- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 194 qdpvfVSLLSLIDQVMVLLGSPGIQLF-------NTFP-RLGAFLrLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQ 265
Cdd:PLN02196 178 -----VALLSIFGKDEVLYREDLKRCYyilekgyNSMPiNLPGTL-FHKSMKARKELAQILAKILSKRRQNGSSHNDLLG 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 266 SYVEALLQQGQEDDPEDMFGeanvlactldMVMAGTETTAATLQWAVFLMVKHPHVQGRV---QEELDRVLGPGQLPQPE 342
Cdd:PLN02196 252 SFMGDKEGLTDEQIADNIIG----------VIFAARDTTASVLTWILKYLAENPSVLEAVteeQMAIRKDKEEGESLTWE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 343 HQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKgrfmK 422
Cdd:PLN02196 322 DTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAP----K 397
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 237681200 423 RGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRL 459
Cdd:PLN02196 398 PNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRW 434
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
294-482 5.92e-19

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 88.87  E-value: 5.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVM-AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTA 372
Cdd:cd20678  244 VDTFMfEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELS 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 373 ADIQL-GGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFldAKGRFMKRG--AFLPFSAGRRVCVGKSLARTELFLL 449
Cdd:cd20678  324 KPVTFpDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRF--SPENSSKRHshAFLPFSAGPRNCIGQQFAMNEMKVA 401
                        170       180       190
                 ....*....|....*....|....*....|...
gi 237681200 450 FAGLLQRYRLLPPPGLSPAdldlrPAPAFTMRP 482
Cdd:cd20678  402 VALTLLRFELLPDPTRIPI-----PIPQLVLKS 429
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
59-483 9.90e-19

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 88.19  E-value: 9.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  59 LMELSERY---GPMFTIHLGSQKTVVLSGYEVVREALvgTGHELADRPPIpIFQHIQRGGGI---------FFSSGARWR 126
Cdd:cd11040    1 LLRNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVF--RNPKTLSFDPI-VIVVVGRVFGSpesakkkegEPGGKGLIR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 127 AGRQFTVRTLQ---SLGVQQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLS 203
Cdd:cd11040   78 LLHDLHKKALSggeGLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELDPDLVEDFW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 204 LIDQVMvllgspgIQLFNTFPRLGAflrlHRPVLSKiEEVRTILRTLLETRRPPLPTG-GPAQSYVEALLQQGQedDPED 282
Cdd:cd11040  158 TFDRGL-------PKLLLGLPRLLA----RKAYAAR-DRLLKALEKYYQAAREERDDGsELIRARAKVLREAGL--SEED 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 283 MfgeANVLACtldMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEH-----QRALPYTSAVLHEV 357
Cdd:cd11040  224 I---ARAELA---LLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltdlLTSCPLLDSTYLET 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 358 QRYiTLLPHVPRCTAADI-QLGGYLLPKGTPV-IPllTSVL-LDKTQWE-TPSQFNPNHFLDAKGRFM---KRGAFLPFS 430
Cdd:cd11040  298 LRL-HSSSTSVRLVTEDTvLGGGYLLRKGSLVmIP--PRLLhMDPEIWGpDPEEFDPERFLKKDGDKKgrgLPGAFRPFG 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 237681200 431 AGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAPAFTMRPP 483
Cdd:cd11040  375 GGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMDESPGLGILPP 427
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
290-451 1.21e-17

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 84.99  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 290 LACT-LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLP-QPEHQRALPYTSAVLHEVQRY---ITLL 364
Cdd:cd11082  221 IAGTlLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPlTLDLLEEMKYTRQVVKEVLRYrppAPMV 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 365 PHVprcTAADIQLG-GYLLPKGTPVIPLLTSVLLDKtqWETPSQFNPNHFLDAKGRFMK-RGAFLPFSAGRRVCVGKSLA 442
Cdd:cd11082  301 PHI---AKKDFPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKyKKNFLVFGAGPHQCVGQEYA 375

                 ....*....
gi 237681200 443 RTELFLLFA 451
Cdd:cd11082  376 INHLMLFLA 384
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
273-463 2.06e-17

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 84.36  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 273 QQGQEDDPEDMFGEAnvlactlDMVM-AGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVL---GPGQLpQPEHQRALP 348
Cdd:cd20679  235 EDGKELSDEDIRAEA-------DTFMfEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLkdrEPEEI-EWDDLAQLP 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 349 YTSAVLHEVQRYITLLPHVPRCTAADIQL-GGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFL 427
Cdd:cd20679  307 FLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFI 386
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 237681200 428 PFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPP 463
Cdd:cd20679  387 PFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDD 422
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
288-464 3.54e-17

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 83.56  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 288 NVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGpGQLPQPEHQRALPYTSAVLHEVQRYITLLPHV 367
Cdd:cd20616  224 NVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFV 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 368 PRCTAADIQLGGYLLPKGTPVIplLTSVLLDKTQ-WETPSQFNPNHFldAKG---RFmkrgaFLPFSAGRRVCVGKSLAR 443
Cdd:cd20616  303 MRKALEDDVIDGYPVKKGTNII--LNIGRMHRLEfFPKPNEFTLENF--EKNvpsRY-----FQPFGFGPRSCVGKYIAM 373
                        170       180
                 ....*....|....*....|.
gi 237681200 444 TELFLLFAGLLQRYRLLPPPG 464
Cdd:cd20616  374 VMMKAILVTLLRRFQVCTLQG 394
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
190-461 4.16e-17

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 83.23  E-value: 4.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 190 RFDYQDPVFVSLlSLIDQVMVLLGSPGIqlfNTFPRlgAFLRLHRPVLSKIEEVRtiLRTLLETRRPPLptggpaQSYVE 269
Cdd:cd20650  146 KFDFLDPLFLSI-TVFPFLTPILEKLNI---SVFPK--DVTNFFYKSVKKIKESR--LDSTQKHRVDFL------QLMID 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 270 AllQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPY 349
Cdd:cd20650  212 S--QNSKETESHKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEY 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 350 TSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPV-IPllTSVL-LDKTQWETPSQFNPNHFLDAKGRFMKRGAFL 427
Cdd:cd20650  290 LDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVmIP--TYALhRDPQYWPEPEEFRPERFSKKNKDNIDPYIYL 367
                        250       260       270
                 ....*....|....*....|....*....|....
gi 237681200 428 PFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLP 461
Cdd:cd20650  368 PFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKP 401
PLN03018 PLN03018
homomethionine N-hydroxylase
35-492 8.77e-17

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 82.75  E-value: 8.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  35 PPGPRPLPFLGNLHLLGVTQQDRALMELS--ERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIq 112
Cdd:PLN03018  42 PPGPPGWPILGNLPELIMTRPRSKYFHLAmkELKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETI- 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 113 rggGIFFSSGARWRAGRQF------------TVRTLQSLGVQQPSMVGKVLQELACLKGQLDSYGGQPLPlALLGWApcn 180
Cdd:PLN03018 121 ---GDNYKSMGTSPYGEQFmkmkkvitteimSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDVRELS-RVYGYA--- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 181 ITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSpgiqLFNTFPRLGAFlrlhRPV-----------LSKIEEVRTILRT 249
Cdd:PLN03018 194 VTMRMLFGRRHVTKENVFSDDGRLGKAEKHHLEV----IFNTLNCLPGF----SPVdyverwlrgwnIDGQEERAKVNVN 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 250 LLETRRPPL---------PTGGPA--QSYVEALLQQgQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKH 318
Cdd:PLN03018 266 LVRSYNNPIidervelwrEKGGKAavEDWLDTFITL-KDQNGKYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKN 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 319 PHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQR------YITllPHVPRctaADIQLGGYLLPKGTPVIPLL 392
Cdd:PLN03018 345 PEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRihpsahYVP--PHVAR---QDTTLGGYFIPKGSHIHVCR 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 393 TSVLLDKTQWETPSQFNPNHFLDAKG------RFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLS 466
Cdd:PLN03018 420 PGLGRNPKIWKDPLVYEPERHLQGDGitkevtLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDFG 499
                        490       500
                 ....*....|....*....|....*.
gi 237681200 467 PADLDLRPAPAFTMRPpaQTLCVVPR 492
Cdd:PLN03018 500 PLSLEEDDASLLMAKP--LLLSVEPR 523
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
242-464 1.00e-16

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 81.79  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 242 EVRTILRTLLETRrpplPTGGPAQS-YVEALLQQGqeddpedmFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPH 320
Cdd:cd20627  167 EMESVLKKVIKER----KGKNFSQHvFIDSLLQGN--------LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEE 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 321 VQGRVQEELDRVLGPGQLpQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKT 400
Cdd:cd20627  235 VQKKLYKEVDQVLGKGPI-TLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNT 313
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 237681200 401 QWETPSQFNPNHFLDAKgrFMKRGAFLPFSaGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPG 464
Cdd:cd20627  314 TWPLPYRFDPDRFDDES--VMKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLLPVDG 374
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
283-463 2.44e-16

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 81.04  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 283 MFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYIT 362
Cdd:cd20649  256 MLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYP 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 363 LLPHVPRCTAADIQLGGYLLPKGTpVIPLLTSVL-LDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSL 441
Cdd:cd20649  336 PAFRFAREAAEDCVVLGQRIPAGA-VLEIPVGFLhHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRL 414
                        170       180
                 ....*....|....*....|..
gi 237681200 442 ARTELFLLFAGLLQRYRLLPPP 463
Cdd:cd20649  415 ALLEIKVTLLHILRRFRFQACP 436
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
231-458 2.32e-15

3-epi-6-deoxocathasterone 23-monooxygenase; Provisional


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 78.24  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 231 RLHRPVLSKIEEVRTILRTLLETRRPPLPTG----GPAQSYVEALLQQGQEDDPEDMFGEANVlactlDMVMAGTETTAA 306
Cdd:PLN03141 195 RLYRSLQAKKRMVKLVKKIIEEKRRAMKNKEedetGIPKDVVDVLLRDGSDELTDDLISDNMI-----DMMIPGEDSVPV 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 307 TLQWAVFLMVKHPHVQGRVQEE---LDRV-LGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLL 382
Cdd:PLN03141 270 LMTLAVKFLSDCPVALQQLTEEnmkLKRLkADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLI 349
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237681200 383 PKGTPVIPLLTSVLLDKTQWETPSQFNPNHFldaKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYR 458
Cdd:PLN03141 350 PKGWCVLAYFRSVHLDEENYDNPYQFNPWRW---QEKDMNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFR 422
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
268-463 1.04e-14

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 75.79  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 268 VEALLQQGQEDDPEDMFG-------EANVLACTLD-MVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLgpgQLP 339
Cdd:cd20615  187 YNRARQRGQSTPIVKLYEavekgdiTFEELLQTLDeMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAR---EQS 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 340 QPEHQRALPYTSAVLH----EVQRYITLLPH-VPRCTAADIQLGGYLLPKGTPVIplLTSVLLDKTQ---WETPSQFNPN 411
Cdd:cd20615  264 GYPMEDYILSTDTLLAycvlESLRLRPLLAFsVPESSPTDKIIGGYRIPANTPVV--VDTYALNINNpfwGPDGEAYRPE 341
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 237681200 412 HFLDAKGRFMkRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPP 463
Cdd:cd20615  342 RFLGISPTDL-RYNFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPD 392
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
223-467 1.13e-14

cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is a heme-containing monooxygenase which participates in epothilone biosynthesis where it catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. This subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 75.54  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPRLGAFL-RLHRPVLSkIEEVRT----------ILRTLLETRRPplptgGPAQSYVEALLQQGQEDDpeDMFGEANVLA 291
Cdd:cd20630  135 FRRFGTATiRLLPPGLD-PEELETaapdvteglaLIEEVIAERRQ-----APVEDDLLTTLLRAEEDG--ERLSEDELMA 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 292 CTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEldrvlgPGQLPQpehqralpytsaVLHEVQRYITLLPH-VPRC 370
Cdd:cd20630  207 LVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE------PELLRN------------ALEEVLRWDNFGKMgTARY 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 371 TAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHfldakgrfmKRGAFLPFSAGRRVCVGKSLARTELFLLF 450
Cdd:cd20630  269 ATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR---------DPNANIAFGYGPHFCIGAALARLELELAV 339
                        250       260
                 ....*....|....*....|
gi 237681200 451 AGLLQRY---RLLPPPGLSP 467
Cdd:cd20630  340 STLLRRFpemELAEPPVFDP 359
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
243-463 2.41e-14

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 74.26  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 243 VRTILRTLLETRRPPLPTGGPA----QSYVEALLQQGQEDDPEDMFGE-------------ANVLACTLDMVMAGTETTA 305
Cdd:cd20629  130 ALAMLRGLSDPPDPDVPAAEAAaaelYDYVLPLIAERRRAPGDDLISRllraevegeklddEEIISFLRLLLPAGSDTTY 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 306 ATLQWAVFLMVKHPHVQGRVQEelDRVLGPgqlpqpehqralpytsAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKG 385
Cdd:cd20629  210 RALANLLTLLLQHPEQLERVRR--DRSLIP----------------AAIEEGLRWEPPVASVPRMALRDVELDGVTIPAG 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 386 TPVIPLLTSVLLDKTQWETPSQFNPnhfldakgrFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRY---RLLPP 462
Cdd:cd20629  272 SLLDLSVGSANRDEDVYPDPDVFDI---------DRKPKPHLVFGGGAHRCLGEHLARVELREALNALLDRLpnlRLDPD 342

                 .
gi 237681200 463 P 463
Cdd:cd20629  343 A 343
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
298-479 4.88e-14

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 74.34  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 298 MAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQ-LPQPEHQRALPYTSAVLHEVQRyitLLPHV----PRCTA 372
Cdd:PLN02426 303 LAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQeAASFEEMKEMHYLHAALYESMR---LFPPVqfdsKFAAE 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 373 ADIQLGGYLLPKGTPVI--PLLTSVLldktqwetPSQFNPNHFLDAKGRFMKRGAFLP--------FSAGRRVCVGKSLA 442
Cdd:PLN02426 380 DDVLPDGTFVAKGTRVTyhPYAMGRM--------ERIWGPDCLEFKPERWLKNGVFVPenpfkypvFQAGLRVCLGKEMA 451
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 237681200 443 RTELFLLFAGLLQRY--RLLPPPGLSPadldlRPAPAFT 479
Cdd:PLN02426 452 LMEMKSVAVAVVRRFdiEVVGRSNRAP-----RFAPGLT 485
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
241-478 1.03e-13

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 72.60  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 241 EEVRTILRTLLETRRpplptGGPAQSYVEALLQQGQEDD--PEDmfgEANVLACTLdmVMAGTETTAATLQWAVFLMVKH 318
Cdd:cd11031  167 QELRGYMAELVAARR-----AEPGDDLLSALVAARDDDDrlSEE---ELVTLAVGL--LVAGHETTASQIGNGVLLLLRH 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 319 PhvqgrvqEELDRVLgpgqlpqpEHQRALPytSAVlHEVQRYITLLPHV--PRCTAADIQLGGYLLPKGTPVIPLLTSVL 396
Cdd:cd11031  237 P-------EQLARLR--------ADPELVP--AAV-EELLRYIPLGAGGgfPRYATEDVELGGVTIRAGEAVLVSLNAAN 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 397 LDKTQWETPSQFNPnhfldakGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYrllppPGL----SPADLDL 472
Cdd:cd11031  299 RDPEVFPDPDRLDL-------DR--EPNPHLAFGHGPHHCLGAPLARLELQVALGALLRRL-----PGLrlavPEEELRW 364

                 ....*.
gi 237681200 473 RPAPAF 478
Cdd:cd11031  365 REGLLT 370
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
288-459 1.15e-13

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 72.83  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 288 NVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEldrVLGPGQLPQPEHQRAL---PYTSAVLHEVQRYITLL 364
Cdd:cd20643  234 DIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAE---VLAARQEAQGDMVKMLksvPLLKAAIKETLRLHPVA 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 365 PHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRgafLPFSAGRRVCVGKSLART 444
Cdd:cd20643  311 VSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN---LGFGFGPRQCLGRRIAET 387
                        170
                 ....*....|....*
gi 237681200 445 ELFLLFAGLLQRYRL 459
Cdd:cd20643  388 EMQLFLIHMLENFKI 402
PLN02971 PLN02971
tryptophan N-hydroxylase
295-458 4.72e-13

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 71.22  E-value: 4.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITL----LPHVprc 370
Cdd:PLN02971 334 ELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVaafnLPHV--- 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 371 TAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFM---KRGAFLPFSAGRRVCVGKSLARTELF 447
Cdd:PLN02971 411 ALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTlteNDLRFISFSTGKRGCAAPALGTAITT 490
                        170
                 ....*....|.
gi 237681200 448 LLFAGLLQRYR 458
Cdd:PLN02971 491 MMLARLLQGFK 501
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
284-458 2.13e-12

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 68.27  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 284 FGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEelDRVLGPgqlpqpehqralpytsAVLHEVQRYITL 363
Cdd:cd11080  189 LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA--DRSLVP----------------RAIAETLRYHPP 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 364 LPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHF-LDAKGRFMKRGAFLPFSAGRRVCVGKSLA 442
Cdd:cd11080  251 VQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREdLGIRSAFSGAADHLAFGSGRHFCVGAALA 330
                        170
                 ....*....|....*.
gi 237681200 443 RTELFLLFAGLLQRYR 458
Cdd:cd11080  331 KREIEIVANQVLDALP 346
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
277-457 2.99e-12

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 68.65  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 277 EDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEL--------------------DRVLGPG 336
Cdd:PLN03195 281 GEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELkalekerakeedpedsqsfnQRVTQFA 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 337 QLPQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAADiqlggYLLPKGTPVIP--LLTSVllDKTQWETPSQFNPNHFL 414
Cdd:PLN03195 361 GLLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGILED-----DVLPDGTKVKAggMVTYV--PYSMGRMEYNWGPDAAS 433
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 237681200 415 DAKGRFMKRGAFLP--------FSAGRRVCVGKSLARTELFLLFAgLLQRY 457
Cdd:PLN03195 434 FKPERWIKDGVFQNaspfkftaFQAGPRICLGKDSAYLQMKMALA-LLCRF 483
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
223-476 3.88e-12

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 68.09  E-value: 3.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 223 FPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPtggpaQSYVEALLQQGQEDDPEDMFgeaNVLACTLDMVMAGTE 302
Cdd:cd11041  170 LPEPRRLRRLLRRARPLIIPEIERRRKLKKGPKEDKP-----NDLLQWLIEAAKGEGERTPY---DLADRQLALSFAAIH 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 303 TTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRALPYTSAVLHEVQRYITLLPH-VPRCTAADIQLG-GY 380
Cdd:cd11041  242 TTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVsLRRKVLKDVTLSdGL 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 381 LLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHF--LDAKGRFMKRGAF-------LPFSAGRRVCVGKSLARTELFLLFA 451
Cdd:cd11041  322 TLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFyrLREQPGQEKKHQFvstspdfLGFGHGRHACPGRFFASNEIKLILA 401
                        250       260
                 ....*....|....*....|....*
gi 237681200 452 GLLQRYRLLPPPGLSpadldlRPAP 476
Cdd:cd11041  402 HLLLNYDFKLPEGGE------RPKN 420
PLN02500 PLN02500
cytochrome P450 90B1
268-458 4.77e-12

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 67.97  E-value: 4.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 268 VEALLQQGQEDDPEDMFGEA---------NVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEE------LDRV 332
Cdd:PLN02500 250 IEKLKEEDESVEEDDLLGWVlkhsnlsteQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEhleiarAKKQ 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 333 LGPGQLPQPEHQRaLPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNP-- 410
Cdd:PLN02500 330 SGESELNWEDYKK-MEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPwr 408
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 237681200 411 -----NHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYR 458
Cdd:PLN02500 409 wqqnnNRGGSSGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFN 461
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
277-484 6.82e-12

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 66.86  E-value: 6.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 277 EDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEldrvlgPGQLPQpehqralpytsAVlHE 356
Cdd:cd11078  198 ADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD------PSLIPN-----------AV-EE 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 357 VQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFN---PNhfldakgrfmkRGAFLPFSAGR 433
Cdd:cd11078  260 TLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDidrPN-----------ARKHLTFGHGI 328
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 237681200 434 RVCVGKSLARTELFLLFAGLLQRYrllppPGLSPADLDLRPAPAFTMRPPA 484
Cdd:cd11078  329 HFCLGAALARMEARIALEELLRRL-----PGMRVPGQEVVYSPSLSFRGPE 374
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
295-446 8.48e-12

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 67.15  E-value: 8.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQ------RALPYTSAVLHEVQRyitLLPHVP 368
Cdd:cd20638  237 ELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKElsmevlEQLKYTGCVIKETLR---LSPPVP 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 369 ---RCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRFMKRGAFLPFSAGRRVCVGKSLARTE 445
Cdd:cd20638  314 ggfRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVL 393

                 .
gi 237681200 446 L 446
Cdd:cd20638  394 L 394
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
64-449 9.27e-12

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 66.78  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  64 ERYGPMFTIHLGSQKTVVLSGYEVVREALVGTgHELAdRPPIPIFQHIQRGGGIFF-SSGARWRAGRQFTVRTLQSLGVQ 142
Cdd:cd20636   20 EKYGNVFKTHLLGRPVIRVTGAENIRKILLGE-HTLV-STQWPQSTRILLGSNTLLnSVGELHRQRRKVLARVFSRAALE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 143 qpSMVGKvLQELacLKGQLDSYGGQPLPLALLGWAPcNITFTL----LFGQRFDYQDpvFVSLLSLIDQVMVLLGSPGIQ 218
Cdd:cd20636   98 --SYLPR-IQDV--VRSEVRGWCRGPGPVAVYTAAK-SLTFRIavriLLGLRLEEQQ--FTYLAKTFEQLVENLFSLPLD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 219 LFNTFPRLGAFLR--LHRPVLSKIEEVrtilrtlLETRRPplptgGPAQSYVEALLQQGQEDDPEDMFGEANVLActLDM 296
Cdd:cd20636  170 VPFSGLRKGIKARdiLHEYMEKAIEEK-------LQRQQA-----AEYCDALDYMIHSARENGKELTMQELKESA--VEL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 297 VMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRvlgPGQLPQPEHQRA---------LPYTSAVLHEVQRyitLLPHV 367
Cdd:cd20636  236 IFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVS---HGLIDQCQCCPGalsleklsrLRYLDCVVKEVLR---LLPPV 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 368 P---RCTAADIQLGGYLLPKGTPVIPLL-----TSVLLDKTQWETPSQFNPNHFLDAKGRFmkrgAFLPFSAGRRVCVGK 439
Cdd:cd20636  310 SggyRTALQTFELDGYQIPKGWSVMYSIrdtheTAAVYQNPEGFDPDRFGVEREESKSGRF----NYIPFGGGVRSCIGK 385
                        410
                 ....*....|
gi 237681200 440 SLARTELFLL 449
Cdd:cd20636  386 ELAQVILKTL 395
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
297-456 2.04e-10

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 62.55  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 297 VMAGTETTAATLQWAVFLMVKHPhvqgrvqEELDRVL-GPGQLPqpehqralpytSAVlHEVQRYITLLPHVPRCTAADI 375
Cdd:cd11033  218 AVAGNETTRNSISGGVLALAEHP-------DQWERLRaDPSLLP-----------TAV-EEILRWASPVIHFRRTATRDT 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 376 QLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQF----NPN-HfldakgrfmkrgafLPFSAGRRVCVGKSLARTELFLLF 450
Cdd:cd11033  279 ELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFditrSPNpH--------------LAFGGGPHFCLGAHLARLELRVLF 344

                 ....*.
gi 237681200 451 AGLLQR 456
Cdd:cd11033  345 EELLDR 350
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
241-481 2.73e-10

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 62.16  E-value: 2.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 241 EEVRTILRTLLETRRPPlptggPAQSYVEALLQQGQEDDPEDmfgEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPh 320
Cdd:cd11029  172 RELVDYLAELVARKRAE-----PGDDLLSALVAARDEGDRLS---EEELVSTVFLLLVAGHETTVNLIGNGVLALLTHP- 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 321 vqgrvqEELDRVL-GPGQLPQpehqralpytsaVLHEVQRYITLLPHVP-RCTAADIQLGGYLLPKGTPVIPLLTSVLLD 398
Cdd:cd11029  243 ------DQLALLRaDPELWPA------------AVEELLRYDGPVALATlRFATEDVEVGGVTIPAGEPVLVSLAAANRD 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 399 KTQWETPSQFNPnhfldakGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYrllppPGLSPADL--DLRPAP 476
Cdd:cd11029  305 PARFPDPDRLDI-------TR--DANGHLAFGHGIHYCLGAPLARLEAEIALGALLTRF-----PDLRLAVPpdELRWRP 370

                 ....*
gi 237681200 477 AFTMR 481
Cdd:cd11029  371 SFLLR 375
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
240-481 2.91e-10

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 61.80  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 240 IEEVRTILRTLLETRRpplptGGPAQSYVEALLQQGQEDDPEDmfgEANVLACTLDMVMAGTETTAATLQWAVFLMVKHP 319
Cdd:cd20625  161 AAELAAYFRDLIARRR-----ADPGDDLISALVAAEEDGDRLS---EDELVANCILLLVAGHETTVNLIGNGLLALLRHP 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 320 HVQGRVQEELDRVlgpgqlpqpehqralpytSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDK 399
Cdd:cd20625  233 EQLALLRADPELI------------------PAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDP 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 400 TQWETPSQFNPnhfldakGRfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYrllppPGLSPADLDLRPAPAFT 479
Cdd:cd20625  295 AVFPDPDRFDI-------TR--APNRHLAFGAGIHFCLGAPLARLEAEIALRALLRRF-----PDLRLLAGEPEWRPSLV 360

                 ..
gi 237681200 480 MR 481
Cdd:cd20625  361 LR 362
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
64-459 4.02e-10

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 61.78  E-value: 4.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200  64 ERYGPMFTIHLGSQKTVVLSGYEVVREALVGTG---HELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSL- 139
Cdd:cd20644    2 QELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGlhpRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSPa 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 140 GVQQ-PSMVGKVLQELA-CLKGQLDSYGGQPLPLALlgwAPCNITFTL------LFGQRFDY--QDPVFVSLlSLIDQVM 209
Cdd:cd20644   82 AVQRfLPMLDAVARDFSqALKKRVLQNARGSLTLDV---QPDLFRFTLeasnlaLYGERLGLvgHSPSSASL-RFISAVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 210 VLLGSPgIQLFNTFPRLgafLRLHRPVLSK--IEEVRTILR----------TLLETRRPPLPTGGPAQsyveaLLQQGQE 277
Cdd:cd20644  158 VMLKTT-VPLLFMPRSL---SRWISPKLWKehFEAWDCIFQyadnciqkiyQELAFGRPQHYTGIVAE-----LLLQAEL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 278 ddPEDMFgEANVLactlDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEldrVLGPGQLPQPEHQRAL---PYTSAVL 354
Cdd:cd20644  229 --SLEAI-KANIT----ELTAGGVDTTAFPLLFTLFELARNPDVQQILRQE---SLAAAAQISEHPQKALtelPLLKAAL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 355 HEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGrfmKRGAF--LPFSAG 432
Cdd:cd20644  299 KETLRLYPVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRG---SGRNFkhLAFGFG 375
                        410       420
                 ....*....|....*....|....*..
gi 237681200 433 RRVCVGKSLARTELFLLFAGLLQRYRL 459
Cdd:cd20644  376 MRQCLGRRLAEAEMLLLLMHVLKNFLV 402
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
267-475 1.08e-09

cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 60.23  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 267 YVEALLQQGQEDDPEDMFG--------------EANVLACTLDMVmAGTETTAATLQWAVFLMVKHPhvqgrvqEELDRV 332
Cdd:cd11030  174 YLDELVARKRREPGDDLLSrlvaehgapgeltdEELVGIAVLLLV-AGHETTANMIALGTLALLEHP-------EQLAAL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 333 LG-PGQLPQpehqralpytsAVlHEVQRYITLLPH-VPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNp 410
Cdd:cd11030  246 RAdPSLVPG-----------AV-EELLRYLSIVQDgLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLD- 312
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 237681200 411 nhfldakgrfMKRGAF--LPFSAGRRVCVGKSLARTELFLLFAGLLQRYrllppPGLSPA----DLDLRPA 475
Cdd:cd11030  313 ----------ITRPARrhLAFGHGVHQCLGQNLARLELEIALPTLFRRF-----PGLRLAvpaeELPFRPD 368
PLN02774 PLN02774
brassinosteroid-6-oxidase
296-458 1.59e-09

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 59.79  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 296 MVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELdrvLGPGQLPQPEHQ------RALPYTSAVLHEVQRYITLLPHVPR 369
Cdd:PLN02774 272 ILYSGYETVSTTSMMAVKYLHDHPKALQELRKEH---LAIRERKRPEDPidwndyKSMRFTRAVIFETSRLATIVNGVLR 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 370 CTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHFLDAKgrFMKRGAFLPFSAGRRVCVGKSLARTELFLL 449
Cdd:PLN02774 349 KTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKS--LESHNYFFLFGGGTRLCPGKELGIVEISTF 426

                 ....*....
gi 237681200 450 FAGLLQRYR 458
Cdd:PLN02774 427 LHYFVTRYR 435
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
244-469 3.52e-09

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 58.71  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 244 RTILRTLLETRRPPLPTGGPAQSYVEAL---LQQGQEDDPEDMFGEANvlACTLDMVMAGTETTAATLQWAVFLMVKHPH 320
Cdd:cd20637  181 RDSLQKSLEKAIREKLQGTQGKDYADALdilIESAKEHGKELTMQELK--DSTIELIFAAFATTASASTSLIMQLLKHPG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 321 VQGRVQEEL--DRVLGPGQLPQPEHQ----RALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLL-- 392
Cdd:cd20637  259 VLEKLREELrsNGILHNGCLCEGTLRldtiSSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIrd 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 393 ---TSVLLDKTQWETPSQFNPNHFLDAKGRFmkrgAFLPFSAGRRVCVGKSLARTELFLLFAGL--LQRY--------RL 459
Cdd:cd20637  339 thdTAPVFKDVDAFDPDRFGQERSEDKDGRF----HYLPFGGGVRTCLGKQLAKLFLKVLAVELasTSRFelatrtfpRM 414
                        250
                 ....*....|
gi 237681200 460 LPPPGLSPAD 469
Cdd:cd20637  415 TTVPVVHPVD 424
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
294-457 4.89e-09

fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 58.48  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 294 LDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEELDRVLgpgqlpQPEHQRALPYTSAVLHEVQRYITLLPHVPRCTAA 373
Cdd:PLN02169 307 FSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKF------DNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAK 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 374 -DIQLGGYLLPKGTPVIPLLTSVLLDKTQW-ETPSQFNPNHFLDAKG--RFMKRGAFLPFSAGRRVCVGKSLARTELFLL 449
Cdd:PLN02169 381 pDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGglRHEPSYKFMAFNSGPRTCLGKHLALLQMKIV 460

                 ....*...
gi 237681200 450 FAGLLQRY 457
Cdd:PLN02169 461 ALEIIKNY 468
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
218-476 4.92e-09

cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 57.99  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 218 QLFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRpplptGGPAQSYVEALLQQgqEDDPEDMFGEANVLACTLdMV 297
Cdd:cd11032  136 ALVSGLGDDSFEEEEVEEMAEALRELNAYLLEHLEERR-----RNPRDDLISRLVEA--EVDGERLTDEEIVGFAIL-LL 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 298 MAGTETTAATLQWAVFLMVKHPHVQGRVQEelDRVLGPGqlpqpehqralpytsaVLHEVQRYITLLPHVPRCTAADIQL 377
Cdd:cd11032  208 IAGHETTTNLLGNAVLCLDEDPEVAARLRA--DPSLIPG----------------AIEEVLRYRPPVQRTARVTTEDVEL 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 378 GGYLLPKGTPVIPLLTSVLLDKTQWETPSQF----NPN-HfldakgrfmkrgafLPFSAGRRVCVGKSLARTELFLLFAG 452
Cdd:cd11032  270 GGVTIPAGQLVIAWLASANRDERQFEDPDTFdidrNPNpH--------------LSFGHGIHFCLGAPLARLEARIALEA 335
                        250       260
                 ....*....|....*....|....
gi 237681200 453 LLQRYRLLPPPglSPADLDLRPAP 476
Cdd:cd11032  336 LLDRFPRIRVD--PDVPLELIDSP 357
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
311-477 7.29e-09

unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 57.47  E-value: 7.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 311 AVFLMVKHPHVQGRVQEELDRVLGPGqlpqpehqrALPYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIP 390
Cdd:cd20624  214 ALALLAAHPEQAARAREEAAVPPGPL---------ARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLI 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 391 LLTSVLLDKTQWETPSQFNPNHFLDakGRFMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPglSPADL 470
Cdd:cd20624  285 FAPFFHRDDEALPFADRFVPEIWLD--GRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLE--SPRSG 360

                 ....*..
gi 237681200 471 DLRPAPA 477
Cdd:cd20624  361 PGEPLPG 367
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
295-464 4.03e-08

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 55.28  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 295 DMVMAGTETTAATLQWAVFLMVKHPhvqgrvqEELDRVlgpgqlpqpehqRALPYT-SAVLHEVQRYITLLPHVPRCTAA 373
Cdd:cd11037  209 DYLSAGLDTTISAIGNALWLLARHP-------DQWERL------------RADPSLaPNAFEEAVRLESPVQTFSRTTTR 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 374 DIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQF----NPN-HfldakgrfmkrgafLPFSAGRRVCVGKSLARTELFL 448
Cdd:cd11037  270 DTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFditrNPSgH--------------VGFGHGVHACVGQHLARLEGEA 335
                        170
                 ....*....|....*.
gi 237681200 449 LFAGLLQRYRLLPPPG 464
Cdd:cd11037  336 LLTALARRVDRIELAG 351
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
236-473 2.11e-07

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 53.14  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 236 VLSKIE----EVRTILRTLLETRRpplptGGPAQSYVEALLQqgqEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWA 311
Cdd:cd11038  166 HLPRIEaaveELYDYADALIEARR-----AEPGDDLISTLVA---AEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 312 VFLMVKHPHVQGRVQEELDrvLGPgqlpqpehqralpytsAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPL 391
Cdd:cd11038  238 MLTFAEHPDQWRALREDPE--LAP----------------AAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLC 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 392 LTSVLLDktqwetPSQFNPNHFlDAKgrfMKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQRY---------RLLPP 462
Cdd:cd11038  300 SHAANRD------PRVFDADRF-DIT---AKRAPHLGFGGGVHHCLGAFLARAELAEALTVLARRLptpaiagepTWLPD 369
                        250
                 ....*....|..
gi 237681200 463 PGLS-PADLDLR 473
Cdd:cd11038  370 SGNTgPATLPLR 381
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
218-442 1.17e-06

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 50.91  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 218 QLFNTFPRLGAFL-RLHRPVLSKIEE-----VRTILRTLLETRRppLPTGGPAQSYVEALLQQGQEDD-PEDMFGEANVL 290
Cdd:cd20634  151 EVYHEFRKLDQLLpKLARGTLSKEEKqeaasVKERLWKLLSPKR--LNRKANRSSWLESYLLHLEEEGvDEEMQARAMLL 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 291 ACTLDMVMAGTETTaatlqWAVFLMVKHPHVQGRVQEELDRVLGPGQLPQPEHQRAL-------PYTSAVLHEVQRyITL 363
Cdd:cd20634  229 QLWATQGNAGPAAF-----WLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVSQTLTINqelldntPVFDSVLSETLR-LTA 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 364 LPHVPRCTAADIQL-----GGYLLPKGTPVI--PLLtSVLLDKTQWETPSQFNPNHFLDA----KGRFMKRGAFL----- 427
Cdd:cd20634  303 APFITREVLQDMKLrladgQEYNLRRGDRLClfPFL-SPQMDPEIHQEPEVFKYDRFLNAdgteKKDFYKNGKRLkyynm 381
                        250
                 ....*....|....*
gi 237681200 428 PFSAGRRVCVGKSLA 442
Cdd:cd20634  382 PWGAGDNVCIGRHFA 396
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
267-461 1.18e-06

P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 50.67  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 267 YVEALLQQGQEDDPEDMFG-------------EANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHVQGRVQEEldrvl 333
Cdd:cd11035  156 YLTPLIAERRANPGDDLISailnaeidgrpltDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRED----- 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 334 gPGQLPqpehqralpytsAVLHEVQRYITLlPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQWETPSQFNPNHf 413
Cdd:cd11035  231 -PELIP------------AAVEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR- 295
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 237681200 414 ldakgrfmKRGAFLPFSAGRRVCVGKSLARTELFLLFAGLLQR---YRLLP 461
Cdd:cd11035  296 --------KPNRHLAFGAGPHRCLGSHLARLELRIALEEWLKRipdFRLAP 338
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
242-461 1.60e-06

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 50.03  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 242 EVRTILRTLLETRRpplptGGPAQSYVEALLQQGQEDDPedmFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPHV 321
Cdd:cd11034  152 ELFGHLRDLIAERR-----ANPRDDLISRLIEGEIDGKP---LSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPED 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 322 QGRVQEELDrvlgpgqlpqpehqrALPytsAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVLLDKTQ 401
Cdd:cd11034  224 RRRLIADPS---------------LIP---NAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEK 285
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237681200 402 WETPSQFNpnhfLDakgRFMKRgaFLPFSAGRRVCVGKSLARTELFLLFAGLLQR---YRLLP 461
Cdd:cd11034  286 FEDPDRID----ID---RTPNR--HLAFGSGVHRCLGSHLARVEARVALTEVLKRipdFELDP 339
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
317-482 2.74e-06

unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 49.28  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 317 KHPHVQGRVQEeldrvlGPGQLPqpehqralpytsAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGTPVIPLLTSVL 396
Cdd:cd11079  212 RHPELQARLRA------NPALLP------------AAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASAN 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 397 LDKTQWETPSQFNPNHFLDAKgrfmkrgafLPFSAGRRVCVGKSLARTELFLLFAGLLQRYRLLPPPGLSPADLDLRPAP 476
Cdd:cd11079  274 RDERVFGDPDEFDPDRHAADN---------LVYGRGIHVCPGAPLARLELRILLEELLAQTEAITLAAGGPPERATYPVG 344

                 ....*.
gi 237681200 477 AFTMRP 482
Cdd:cd11079  345 GYASVP 350
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
310-457 3.19e-04

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 43.07  E-value: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 310 WAVFLMVKHPHVQGRVQEELDRVLGpGQLPQP-----EHQRALPYT-SAVLHEvqryITLLP--HVPRCTAADIQLGGYL 381
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLG-KAGKDKikiseDDLKKMPYIkRCVLEA----IRLRSpgAITRKVVKPIKIKNYT 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 382 LPKGTpviPLLTSVLL---DKTQWETPSQFNPNHFLDA---KGRFMKrgAFLPFSAGRRVCVGKSLARTELFLLFAGLLQ 455
Cdd:cd20635  307 IPAGD---MLMLSPYWahrNPKYFPDPELFKPERWKKAdleKNVFLE--GFVAFGGGRYQCPGRWFALMEIQMFVAMFLY 381

                 ..
gi 237681200 456 RY 457
Cdd:cd20635  382 KY 383
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
310-477 5.00e-04

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 42.52  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 310 WAVFL---MVKHPHVQGRVQEELDRvlgpgqlpqpehqralpYTSAVLHEVQRYITLLPHVPRCTAADIQLGGYLLPKGT 386
Cdd:cd11067  239 FVTFAalaLHEHPEWRERLRSGDED-----------------YAEAFVQEVRRFYPFFPFVGARARRDFEWQGYRFPKGQ 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237681200 387 PVIPLLTSVLLDKTQWETPSQFNPNHFLDAKGRfmkRGAFLP-----FSAGRRvCVGKSLArTELFLLFAGLLQR--YRL 459
Cdd:cd11067  302 RVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGD---PFDFIPqgggdHATGHR-CPGEWIT-IALMKEALRLLARrdYYD 376
                        170
                 ....*....|....*...
gi 237681200 460 LPPPGLSpadLDLRPAPA 477
Cdd:cd11067  377 VPPQDLS---IDLNRMPA 391
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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